3zfv

Crystal structure of an archaeal CRISPR-associated Cas6 nuclease

spinqualitylabelsall models 3zfv, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3zfv is a 4 chain structure with sequence from Atcc 35091. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL NonStd Res: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CAS6A_SULSO] CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). Publication Abstract from PubMed The competition between viruses and hosts is played out in all branches of life. Many prokaryotes have an adaptive immune system termed "CRISPR" which is based on the capture of short pieces of viral DNA. The captured DNA is integrated into the genomic DNA of the organism flanked by direct repeats, transcribed and processed to generate CRISPR RNA (crRNA) that is loaded into a variety of effector complexes. These complexes carry out sequence-specific detection and destruction of invading mobile genetic elements. Here we report the structure and activity of a Cas6 enzyme (Sso1437) from Sulfolobus solfataricus responsible for the generation of unit-length crRNA species. The crystal structure reveals an unusual dimeric organisation that is important for the enzyme's activity. In addition, the active site lacks the canonical catalytic histidine residue that has been viewed as an essential feature of the Cas6 family. Although several residues contribute towards catalysis, none is absolutely essential. Coupled with the very low catalytic rate constants of the Cas6 family and the plasticity of the active site, this suggests that the crRNA recognition and chaperone-like activities of the Cas6 family should be considered as equal to or even more important than their role as traditional enzymes. Structure of a dimeric crenarchaeal Cas6 enzyme with an atypical active site for CRISPR RNA processing.,Reeks J, Sokolowski RD, Graham S, Liu H, Naismith JH, White MF Biochem J. 2013 Mar 25. PMID:23527601 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also CRISPR subtype I-A Endonuclease

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