5j72 | pdb_00005j72

Cwp6 from Clostridium difficile

spinqualitylabelsall models 5j72, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5j72 is a 2 chain structure with sequence from Clostridioides difficile 630. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, CIT, CL, NA, ZN Gene: cwp6, CD630_27840 (Clostridioides difficile 630) Activity: N-acetylmuramoyl-L-alanine amidase, with EC number 3.5.1.28 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Bacterial cell wall proteins play crucial roles in cell survival, growth, and environmental interactions. In Gram-positive bacteria, cell wall proteins include several types that are non-covalently attached via cell wall binding domains. Of the two conserved surface-layer (S-layer)-anchoring modules composed of three tandem SLH or CWB2 domains, the latter have so far eluded structural insight. The crystal structures of Cwp8 and Cwp6 reveal multi-domain proteins, each containing an embedded CWB2 module. It consists of a triangular trimer of Rossmann-fold CWB2 domains, a feature common to 29 cell wall proteins in Clostridium difficile 630. The structural basis of the intact module fold necessary for its binding to the cell wall is revealed. A comparison with previously reported atomic force microscopy data of S-layers suggests that C. difficile S-layers are complex oligomeric structures, likely composed of several different proteins. The CWB2 Cell Wall-Anchoring Module Is Revealed by the Crystal Structures of the Clostridium difficile Cell Wall Proteins Cwp8 and Cwp6.,Usenik A, Renko M, Mihelic M, Lindic N, Borisek J, Perdih A, Pretnar G, Muller U, Turk D Structure. 2017 Mar 7;25(3):514-521. doi: 10.1016/j.str.2016.12.018. Epub 2017, Jan 26. PMID:28132783 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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