High-resolution crystal structure of the anti-CRISPR protein AcrIC5

As a result of the long-term battle of bacteria and archaea against invaders such as viruses and genetic mobile elements, they have developed CRISPR-Cas systems for self-defense, which allows them to remove the viral genetic material introduced into host cells via infection. To fight against this ba...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Kang, Yong Jun [verfasserIn] Park, Hyun Ho [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2022

Schlagwörter:	Anti-CRISPR AcrIC5 Adaptive immunity CRISPR-Cas system Crystal structure Type I–C cascade

Übergeordnetes Werk:	Enthalten in: Biochemical and biophysical research communications - Orlando, Fla. : Academic Press, 1959, 625, Seite 102-108
Übergeordnetes Werk:	volume:625 ; pages:102-108

DOI / URN:	10.1016/j.bbrc.2022.08.005

Katalog-ID:	ELV008374732

Internformat


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100	1		\|a Kang, Yong Jun \|e verfasserin \|0 (orcid)0000-0001-9317-5499 \|4 aut
245	1	0	\|a High-resolution crystal structure of the anti-CRISPR protein AcrIC5
264		1	\|c 2022
336			\|a nicht spezifiziert \|b zzz \|2 rdacontent
337			\|a Computermedien \|b c \|2 rdamedia
338			\|a Online-Ressource \|b cr \|2 rdacarrier
520			\|a As a result of the long-term battle of bacteria and archaea against invaders such as viruses and genetic mobile elements, they have developed CRISPR-Cas systems for self-defense, which allows them to remove the viral genetic material introduced into host cells via infection. To fight against this bacterial immune system, however, viruses have also evolved to produce multiple anti-CRISPR proteins that can inhibit the bacterial CRISPR-Cas system. In this study, we introduced a tentative inhibitory activity against a type I–C CRISPR-Cas system by determining the crystal structure of AcrIC5 from Pseudomonas delhiensis. Structural analysis revealed that AcrIC5 was composed of noble folds comprising two antiparallel sheets and three helices. Although AcrIC5 did not directly interact with either the type I–C cascade from Neisseria lactamia or the type I–F cascade from Pseudomonas aeruginosa in our analysis, a highly acidic surface feature indicated that AcrIC5 may be DNA mimic Acrs that directly binds to the target DNA binding site in type I–C cascade and inhibits the recruitment of the target DNA to this cascade.
650		4	\|a Anti-CRISPR
650		4	\|a AcrIC5
650		4	\|a Adaptive immunity
650		4	\|a CRISPR-Cas system
650		4	\|a Crystal structure
650		4	\|a Type I–C cascade
700	1		\|a Park, Hyun Ho \|e verfasserin \|0 (orcid)0000-0001-9928-0847 \|4 aut
773	0	8	\|i Enthalten in \|t Biochemical and biophysical research communications \|d Orlando, Fla. : Academic Press, 1959 \|g 625, Seite 102-108 \|h Online-Ressource \|w (DE-627)254231691 \|w (DE-600)1461396-7 \|w (DE-576)103373039 \|x 0006-291X \|7 nnns
773	1	8	\|g volume:625 \|g pages:102-108
912			\|a GBV_USEFLAG_U
912			\|a SYSFLAG_U
912			\|a GBV_ELV
912			\|a FID-BIODIV
912			\|a SSG-OLC-PHA
912			\|a GBV_ILN_20
912			\|a GBV_ILN_22
912			\|a GBV_ILN_23
912			\|a GBV_ILN_24
912			\|a GBV_ILN_31
912			\|a GBV_ILN_32
912			\|a GBV_ILN_40
912			\|a GBV_ILN_60
912			\|a GBV_ILN_62
912			\|a GBV_ILN_63
912			\|a GBV_ILN_65
912			\|a GBV_ILN_69
912			\|a GBV_ILN_70
912			\|a GBV_ILN_73
912			\|a GBV_ILN_74
912			\|a GBV_ILN_90
912			\|a GBV_ILN_95
912			\|a GBV_ILN_100
912			\|a GBV_ILN_101
912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
912			\|a GBV_ILN_151
912			\|a GBV_ILN_224
912			\|a GBV_ILN_252
912			\|a GBV_ILN_370
912			\|a GBV_ILN_602
912			\|a GBV_ILN_702
912			\|a GBV_ILN_2003
912			\|a GBV_ILN_2004
912			\|a GBV_ILN_2005
912			\|a GBV_ILN_2011
912			\|a GBV_ILN_2014
912			\|a GBV_ILN_2015
912			\|a GBV_ILN_2020
912			\|a GBV_ILN_2021
912			\|a GBV_ILN_2025
912			\|a GBV_ILN_2027
912			\|a GBV_ILN_2034
912			\|a GBV_ILN_2038
912			\|a GBV_ILN_2044
912			\|a GBV_ILN_2048
912			\|a GBV_ILN_2049
912			\|a GBV_ILN_2050
912			\|a GBV_ILN_2056
912			\|a GBV_ILN_2059
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2064
912			\|a GBV_ILN_2065
912			\|a GBV_ILN_2068
912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2112
912			\|a GBV_ILN_2113
912			\|a GBV_ILN_2118
912			\|a GBV_ILN_2122
912			\|a GBV_ILN_2129
912			\|a GBV_ILN_2143
912			\|a GBV_ILN_2147
912			\|a GBV_ILN_2148
912			\|a GBV_ILN_2152
912			\|a GBV_ILN_2153
912			\|a GBV_ILN_2190
912			\|a GBV_ILN_2336
912			\|a GBV_ILN_2507
912			\|a GBV_ILN_2522
912			\|a GBV_ILN_4035
912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4126
912			\|a GBV_ILN_4242
912			\|a GBV_ILN_4251
912			\|a GBV_ILN_4305
912			\|a GBV_ILN_4313
912			\|a GBV_ILN_4323
912			\|a GBV_ILN_4324
912			\|a GBV_ILN_4326
912			\|a GBV_ILN_4333
912			\|a GBV_ILN_4334
912			\|a GBV_ILN_4335
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4393
936	b	k	\|a 35.70 \|j Biochemie: Allgemeines
936	b	k	\|a 42.12 \|j Biophysik
951			\|a AR
952			\|d 625 \|h 102-108

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matchkey_str	article:0006291X:2022----::iheouinrsasrcuefhatci
hierarchy_sort_str	2022
bklnumber	35.70 42.12
publishDate	2022
allfields	10.1016/j.bbrc.2022.08.005 doi (DE-627)ELV008374732 (ELSEVIER)S0006-291X(22)01110-X DE-627 ger DE-627 rda eng 570 DE-600 BIODIV DE-30 fid 35.70 bkl 42.12 bkl Kang, Yong Jun verfasserin (orcid)0000-0001-9317-5499 aut High-resolution crystal structure of the anti-CRISPR protein AcrIC5 2022 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier As a result of the long-term battle of bacteria and archaea against invaders such as viruses and genetic mobile elements, they have developed CRISPR-Cas systems for self-defense, which allows them to remove the viral genetic material introduced into host cells via infection. To fight against this bacterial immune system, however, viruses have also evolved to produce multiple anti-CRISPR proteins that can inhibit the bacterial CRISPR-Cas system. In this study, we introduced a tentative inhibitory activity against a type I–C CRISPR-Cas system by determining the crystal structure of AcrIC5 from Pseudomonas delhiensis. Structural analysis revealed that AcrIC5 was composed of noble folds comprising two antiparallel sheets and three helices. Although AcrIC5 did not directly interact with either the type I–C cascade from Neisseria lactamia or the type I–F cascade from Pseudomonas aeruginosa in our analysis, a highly acidic surface feature indicated that AcrIC5 may be DNA mimic Acrs that directly binds to the target DNA binding site in type I–C cascade and inhibits the recruitment of the target DNA to this cascade. Anti-CRISPR AcrIC5 Adaptive immunity CRISPR-Cas system Crystal structure Type I–C cascade Park, Hyun Ho verfasserin (orcid)0000-0001-9928-0847 aut Enthalten in Biochemical and biophysical research communications Orlando, Fla. : Academic Press, 1959 625, Seite 102-108 Online-Ressource (DE-627)254231691 (DE-600)1461396-7 (DE-576)103373039 0006-291X nnns volume:625 pages:102-108 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_252 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.70 Biochemie: Allgemeines 42.12 Biophysik AR 625 102-108
spelling	10.1016/j.bbrc.2022.08.005 doi (DE-627)ELV008374732 (ELSEVIER)S0006-291X(22)01110-X DE-627 ger DE-627 rda eng 570 DE-600 BIODIV DE-30 fid 35.70 bkl 42.12 bkl Kang, Yong Jun verfasserin (orcid)0000-0001-9317-5499 aut High-resolution crystal structure of the anti-CRISPR protein AcrIC5 2022 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier As a result of the long-term battle of bacteria and archaea against invaders such as viruses and genetic mobile elements, they have developed CRISPR-Cas systems for self-defense, which allows them to remove the viral genetic material introduced into host cells via infection. To fight against this bacterial immune system, however, viruses have also evolved to produce multiple anti-CRISPR proteins that can inhibit the bacterial CRISPR-Cas system. In this study, we introduced a tentative inhibitory activity against a type I–C CRISPR-Cas system by determining the crystal structure of AcrIC5 from Pseudomonas delhiensis. Structural analysis revealed that AcrIC5 was composed of noble folds comprising two antiparallel sheets and three helices. Although AcrIC5 did not directly interact with either the type I–C cascade from Neisseria lactamia or the type I–F cascade from Pseudomonas aeruginosa in our analysis, a highly acidic surface feature indicated that AcrIC5 may be DNA mimic Acrs that directly binds to the target DNA binding site in type I–C cascade and inhibits the recruitment of the target DNA to this cascade. Anti-CRISPR AcrIC5 Adaptive immunity CRISPR-Cas system Crystal structure Type I–C cascade Park, Hyun Ho verfasserin (orcid)0000-0001-9928-0847 aut Enthalten in Biochemical and biophysical research communications Orlando, Fla. : Academic Press, 1959 625, Seite 102-108 Online-Ressource (DE-627)254231691 (DE-600)1461396-7 (DE-576)103373039 0006-291X nnns volume:625 pages:102-108 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_252 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.70 Biochemie: Allgemeines 42.12 Biophysik AR 625 102-108
allfields_unstemmed	10.1016/j.bbrc.2022.08.005 doi (DE-627)ELV008374732 (ELSEVIER)S0006-291X(22)01110-X DE-627 ger DE-627 rda eng 570 DE-600 BIODIV DE-30 fid 35.70 bkl 42.12 bkl Kang, Yong Jun verfasserin (orcid)0000-0001-9317-5499 aut High-resolution crystal structure of the anti-CRISPR protein AcrIC5 2022 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier As a result of the long-term battle of bacteria and archaea against invaders such as viruses and genetic mobile elements, they have developed CRISPR-Cas systems for self-defense, which allows them to remove the viral genetic material introduced into host cells via infection. To fight against this bacterial immune system, however, viruses have also evolved to produce multiple anti-CRISPR proteins that can inhibit the bacterial CRISPR-Cas system. In this study, we introduced a tentative inhibitory activity against a type I–C CRISPR-Cas system by determining the crystal structure of AcrIC5 from Pseudomonas delhiensis. Structural analysis revealed that AcrIC5 was composed of noble folds comprising two antiparallel sheets and three helices. Although AcrIC5 did not directly interact with either the type I–C cascade from Neisseria lactamia or the type I–F cascade from Pseudomonas aeruginosa in our analysis, a highly acidic surface feature indicated that AcrIC5 may be DNA mimic Acrs that directly binds to the target DNA binding site in type I–C cascade and inhibits the recruitment of the target DNA to this cascade. Anti-CRISPR AcrIC5 Adaptive immunity CRISPR-Cas system Crystal structure Type I–C cascade Park, Hyun Ho verfasserin (orcid)0000-0001-9928-0847 aut Enthalten in Biochemical and biophysical research communications Orlando, Fla. : Academic Press, 1959 625, Seite 102-108 Online-Ressource (DE-627)254231691 (DE-600)1461396-7 (DE-576)103373039 0006-291X nnns volume:625 pages:102-108 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_252 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.70 Biochemie: Allgemeines 42.12 Biophysik AR 625 102-108
allfieldsGer	10.1016/j.bbrc.2022.08.005 doi (DE-627)ELV008374732 (ELSEVIER)S0006-291X(22)01110-X DE-627 ger DE-627 rda eng 570 DE-600 BIODIV DE-30 fid 35.70 bkl 42.12 bkl Kang, Yong Jun verfasserin (orcid)0000-0001-9317-5499 aut High-resolution crystal structure of the anti-CRISPR protein AcrIC5 2022 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier As a result of the long-term battle of bacteria and archaea against invaders such as viruses and genetic mobile elements, they have developed CRISPR-Cas systems for self-defense, which allows them to remove the viral genetic material introduced into host cells via infection. To fight against this bacterial immune system, however, viruses have also evolved to produce multiple anti-CRISPR proteins that can inhibit the bacterial CRISPR-Cas system. In this study, we introduced a tentative inhibitory activity against a type I–C CRISPR-Cas system by determining the crystal structure of AcrIC5 from Pseudomonas delhiensis. Structural analysis revealed that AcrIC5 was composed of noble folds comprising two antiparallel sheets and three helices. Although AcrIC5 did not directly interact with either the type I–C cascade from Neisseria lactamia or the type I–F cascade from Pseudomonas aeruginosa in our analysis, a highly acidic surface feature indicated that AcrIC5 may be DNA mimic Acrs that directly binds to the target DNA binding site in type I–C cascade and inhibits the recruitment of the target DNA to this cascade. Anti-CRISPR AcrIC5 Adaptive immunity CRISPR-Cas system Crystal structure Type I–C cascade Park, Hyun Ho verfasserin (orcid)0000-0001-9928-0847 aut Enthalten in Biochemical and biophysical research communications Orlando, Fla. : Academic Press, 1959 625, Seite 102-108 Online-Ressource (DE-627)254231691 (DE-600)1461396-7 (DE-576)103373039 0006-291X nnns volume:625 pages:102-108 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_252 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.70 Biochemie: Allgemeines 42.12 Biophysik AR 625 102-108
allfieldsSound	10.1016/j.bbrc.2022.08.005 doi (DE-627)ELV008374732 (ELSEVIER)S0006-291X(22)01110-X DE-627 ger DE-627 rda eng 570 DE-600 BIODIV DE-30 fid 35.70 bkl 42.12 bkl Kang, Yong Jun verfasserin (orcid)0000-0001-9317-5499 aut High-resolution crystal structure of the anti-CRISPR protein AcrIC5 2022 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier As a result of the long-term battle of bacteria and archaea against invaders such as viruses and genetic mobile elements, they have developed CRISPR-Cas systems for self-defense, which allows them to remove the viral genetic material introduced into host cells via infection. To fight against this bacterial immune system, however, viruses have also evolved to produce multiple anti-CRISPR proteins that can inhibit the bacterial CRISPR-Cas system. In this study, we introduced a tentative inhibitory activity against a type I–C CRISPR-Cas system by determining the crystal structure of AcrIC5 from Pseudomonas delhiensis. Structural analysis revealed that AcrIC5 was composed of noble folds comprising two antiparallel sheets and three helices. Although AcrIC5 did not directly interact with either the type I–C cascade from Neisseria lactamia or the type I–F cascade from Pseudomonas aeruginosa in our analysis, a highly acidic surface feature indicated that AcrIC5 may be DNA mimic Acrs that directly binds to the target DNA binding site in type I–C cascade and inhibits the recruitment of the target DNA to this cascade. Anti-CRISPR AcrIC5 Adaptive immunity CRISPR-Cas system Crystal structure Type I–C cascade Park, Hyun Ho verfasserin (orcid)0000-0001-9928-0847 aut Enthalten in Biochemical and biophysical research communications Orlando, Fla. : Academic Press, 1959 625, Seite 102-108 Online-Ressource (DE-627)254231691 (DE-600)1461396-7 (DE-576)103373039 0006-291X nnns volume:625 pages:102-108 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_252 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.70 Biochemie: Allgemeines 42.12 Biophysik AR 625 102-108
language	English
source	Enthalten in Biochemical and biophysical research communications 625, Seite 102-108 volume:625 pages:102-108
sourceStr	Enthalten in Biochemical and biophysical research communications 625, Seite 102-108 volume:625 pages:102-108
format_phy_str_mv	Article
bklname	Biochemie: Allgemeines Biophysik
institution	findex.gbv.de
topic_facet	Anti-CRISPR AcrIC5 Adaptive immunity CRISPR-Cas system Crystal structure Type I–C cascade
dewey-raw	570
isfreeaccess_bool	false
container_title	Biochemical and biophysical research communications
authorswithroles_txt_mv	Kang, Yong Jun @@aut@@ Park, Hyun Ho @@aut@@
publishDateDaySort_date	2022-01-01T00:00:00Z
hierarchy_top_id	254231691
dewey-sort	3570
id	ELV008374732
language_de	englisch
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author	Kang, Yong Jun
spellingShingle	Kang, Yong Jun ddc 570 fid BIODIV bkl 35.70 bkl 42.12 misc Anti-CRISPR misc AcrIC5 misc Adaptive immunity misc CRISPR-Cas system misc Crystal structure misc Type I–C cascade High-resolution crystal structure of the anti-CRISPR protein AcrIC5
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topic_title	570 DE-600 BIODIV DE-30 fid 35.70 bkl 42.12 bkl High-resolution crystal structure of the anti-CRISPR protein AcrIC5 Anti-CRISPR AcrIC5 Adaptive immunity CRISPR-Cas system Crystal structure Type I–C cascade
topic	ddc 570 fid BIODIV bkl 35.70 bkl 42.12 misc Anti-CRISPR misc AcrIC5 misc Adaptive immunity misc CRISPR-Cas system misc Crystal structure misc Type I–C cascade
topic_unstemmed	ddc 570 fid BIODIV bkl 35.70 bkl 42.12 misc Anti-CRISPR misc AcrIC5 misc Adaptive immunity misc CRISPR-Cas system misc Crystal structure misc Type I–C cascade
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title	High-resolution crystal structure of the anti-CRISPR protein AcrIC5
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title_full	High-resolution crystal structure of the anti-CRISPR protein AcrIC5
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journal	Biochemical and biophysical research communications
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author_browse	Kang, Yong Jun Park, Hyun Ho
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title_sort	high-resolution crystal structure of the anti-crispr protein acric5
title_auth	High-resolution crystal structure of the anti-CRISPR protein AcrIC5
abstract	As a result of the long-term battle of bacteria and archaea against invaders such as viruses and genetic mobile elements, they have developed CRISPR-Cas systems for self-defense, which allows them to remove the viral genetic material introduced into host cells via infection. To fight against this bacterial immune system, however, viruses have also evolved to produce multiple anti-CRISPR proteins that can inhibit the bacterial CRISPR-Cas system. In this study, we introduced a tentative inhibitory activity against a type I–C CRISPR-Cas system by determining the crystal structure of AcrIC5 from Pseudomonas delhiensis. Structural analysis revealed that AcrIC5 was composed of noble folds comprising two antiparallel sheets and three helices. Although AcrIC5 did not directly interact with either the type I–C cascade from Neisseria lactamia or the type I–F cascade from Pseudomonas aeruginosa in our analysis, a highly acidic surface feature indicated that AcrIC5 may be DNA mimic Acrs that directly binds to the target DNA binding site in type I–C cascade and inhibits the recruitment of the target DNA to this cascade.
abstractGer	As a result of the long-term battle of bacteria and archaea against invaders such as viruses and genetic mobile elements, they have developed CRISPR-Cas systems for self-defense, which allows them to remove the viral genetic material introduced into host cells via infection. To fight against this bacterial immune system, however, viruses have also evolved to produce multiple anti-CRISPR proteins that can inhibit the bacterial CRISPR-Cas system. In this study, we introduced a tentative inhibitory activity against a type I–C CRISPR-Cas system by determining the crystal structure of AcrIC5 from Pseudomonas delhiensis. Structural analysis revealed that AcrIC5 was composed of noble folds comprising two antiparallel sheets and three helices. Although AcrIC5 did not directly interact with either the type I–C cascade from Neisseria lactamia or the type I–F cascade from Pseudomonas aeruginosa in our analysis, a highly acidic surface feature indicated that AcrIC5 may be DNA mimic Acrs that directly binds to the target DNA binding site in type I–C cascade and inhibits the recruitment of the target DNA to this cascade.
abstract_unstemmed	As a result of the long-term battle of bacteria and archaea against invaders such as viruses and genetic mobile elements, they have developed CRISPR-Cas systems for self-defense, which allows them to remove the viral genetic material introduced into host cells via infection. To fight against this bacterial immune system, however, viruses have also evolved to produce multiple anti-CRISPR proteins that can inhibit the bacterial CRISPR-Cas system. In this study, we introduced a tentative inhibitory activity against a type I–C CRISPR-Cas system by determining the crystal structure of AcrIC5 from Pseudomonas delhiensis. Structural analysis revealed that AcrIC5 was composed of noble folds comprising two antiparallel sheets and three helices. Although AcrIC5 did not directly interact with either the type I–C cascade from Neisseria lactamia or the type I–F cascade from Pseudomonas aeruginosa in our analysis, a highly acidic surface feature indicated that AcrIC5 may be DNA mimic Acrs that directly binds to the target DNA binding site in type I–C cascade and inhibits the recruitment of the target DNA to this cascade.
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title_short	High-resolution crystal structure of the anti-CRISPR protein AcrIC5
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up_date	2024-07-06T19:29:07.119Z
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score	7.4006405

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High-resolution crystal structure of the anti-CRISPR protein AcrIC5

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