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
Autor*in: |
Kang, Yong Jun [verfasserIn] Park, Hyun Ho [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2022 |
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Schlagwörter: |
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Übergeordnetes Werk: |
Enthalten in: Biochemical and biophysical research communications - Orlando, Fla. : Academic Press, 1959, 625, Seite 102-108 |
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Übergeordnetes Werk: |
volume:625 ; pages:102-108 |
DOI / URN: |
10.1016/j.bbrc.2022.08.005 |
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Katalog-ID: |
ELV008374732 |
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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 | ||
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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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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 |
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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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Kang, Yong Jun |
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Biochemical and biophysical research communications |
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Kang, Yong Jun Park, Hyun Ho |
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Elektronische Aufsätze |
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Kang, Yong Jun |
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10.1016/j.bbrc.2022.08.005 |
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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. |
collection_details |
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title_short |
High-resolution crystal structure of the anti-CRISPR protein AcrIC5 |
remote_bool |
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author2 |
Park, Hyun Ho |
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doi_str |
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up_date |
2024-07-06T19:29:07.119Z |
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