5jip

Crystal structure of the Clostridium perfringens spore cortex lytic enzyme SleM

spinqualitylabelsall models 5jip, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5jip is a 2 chain structure with sequence from Clostridium perfringens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: MES, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O06496_CLOPF Publication Abstract from PubMed Clostridium perfringens spores employ two peptidoglycan lysins to degrade the spore cortex during germination. SleC initiates cortex hydrolysis to generate cortical fragments that are degraded further by the muramidase SleM. Here, we present the crystal structure of the C. perfringens S40 SleM protein at 1.8 A. SleM comprises an N-terminal catalytic domain that adopts an irregular alpha/beta-barrel fold that is common to GH25 family lysozymes, plus a C-terminal fibronectin type III domain. The latter is involved in forming the SleM dimer that is evident in both the crystal structure and in solution. A truncated form of SleM that lacks the FnIII domain shows reduced activity against spore sacculi indicating that this domain may have a role in facilitating the position of substrate with respect to the enzyme's active site. Proteins 2016. (c) 2016 Wiley Periodicals, Inc. The crystal structure of Clostridium perfringens SleM, a muramidase involved in cortical hydrolysis during spore germination.,Al-Riyami B, Ustok FI, Stott K, Chirgadze DY, Christie G Proteins. 2016 Aug 2. doi: 10.1002/prot.25112. PMID:27488615 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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