7vjo

Pectobacterium phage ZF40 apo-Aca2

spinqualitylabelsall models 7vjo, resolution 1.31Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7vjo is a 2 chain structure with sequence from Pectobacterium phage ZF40. This structure supersedes the now removed PDB entry 7cq8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.31Å Ligands: CL, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function H9C180_9CAUD Publication Abstract from PubMed It has been shown that phages have evolved anti-CRISPR (Acr) proteins to inhibit host CRISPR-Cas systems. Most acr genes are located upstream of anti-CRISPR-associated (aca) genes, which is instrumental for identifying these acr genes. Thus far, eight Aca families (Aca1-Aca8) have been identified, all proteins of which share low sequence homology and bind to different target DNA sequences. Recently, Aca1 and Aca2 proteins were discovered to function as repressors by binding to acr-aca promoters, thus implying a potential anti-anti-CRISPR mechanism. However, the structural basis for the repression roles of Aca proteins is still unknown. Here, we elucidated apo-structures of Aca1 and Aca2 proteins and their complex structures with their cognate operator DNA in two model systems, the Pseudomonas phage JBD30 and the Pectobacterium carotovorum template phage ZF40. In combination with biochemical and cellular assays, our study unveils dimerization and DNA-recognition mechanisms of Aca1 and Aca2 family proteins, thus revealing the molecular basis for Aca1-and Aca2-mediated anti-CRISPR repression. Our results also shed light on understanding the repression roles of other Aca family proteins and autoregulation roles of acr-aca operons. Structural basis for anti-CRISPR repression mediated by bacterial operon proteins Aca1 and Aca2.,Liu Y, Zhang L, Guo M, Chen L, Wu B, Huang H J Biol Chem. 2021 Dec;297(6):101357. doi: 10.1016/j.jbc.2021.101357. Epub 2021, Oct 28. PMID:34756887 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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