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8JI9

Crystal Structure of cas7 and AcrIE10 complex

Summary for 8JI9
Entry DOI10.2210/pdb8ji9/pdb
Descriptortype I-E Cascade subunit cas7, Uncharacterized protein (3 entities in total)
Functional Keywordscrispr, cas7, acr, cascade, acrie10, antimicrobial protein
Biological sourceKlebsiella pneumoniae
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Total number of polymer chains4
Total formula weight96875.55
Authors
Zhang, Y.,Yu, C.Z.,Sun, S.Y. (deposition date: 2023-05-26, release date: 2024-07-24, Last modification date: 2024-08-28)
Primary citationJiang, C.,Yu, C.,Sun, S.,Lin, J.,Cai, M.,Wei, Z.,Feng, L.,Li, J.,Zhang, Y.,Dong, K.,Guo, X.,Qin, J.,Zhang, Y.
A new anti-CRISPR gene promotes the spread of drug-resistance plasmids in Klebsiella pneumoniae.
Nucleic Acids Res., 52:8370-8384, 2024
Cited by
PubMed Abstract: The Klebsiella pneumoniae (K. pneumoniae, Kp) populations carrying both resistance-encoding and virulence-encoding mobile genetic elements (MGEs) significantly threaten global health. In this study, we identified a new anti-CRISPR gene (acrIE10) on a conjugative plasmid with self-target sequence in K. pneumoniae with type I-E* CRISPR-Cas system. AcrIE10 interacts with the Cas7* subunit of K. pneumoniae I-E* CRISPR-Cas system. The crystal structure of the AcrIE10-KpCas7* complex suggests that AcrIE10 suppresses the I-E* CRISPR-Cas by binding directly to Cas7 to prevent its hexamerization, thereby preventing the surveillance complex assembly and crRNA loading. Bioinformatic and functional analyses revealed that AcrIE10 is functionally widespread across diverse species. Our study reports a novel anti-CRISPR and highlights its potential role in spreading resistance and virulence among pathogens.
PubMed: 38888121
DOI: 10.1093/nar/gkae516
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.54 Å)
Structure validation

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