5JIP: Crystal structure of the Clostridium perfringens spore cortex lytic enzyme SleM

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; 84:1681-1689. (c) 2016 Wiley Periodicals, Inc.
PDB ID: 5JIPDownload
MMDB ID: 142149
PDB Deposition Date: 2016/4/22
Updated in MMDB: 2016/11
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 5JIP: dimeric; determined by author and by software (PISA)
Molecular Components in 5JIP
Label Count Molecule
Proteins (2 molecules)
Cortical-lytic Enzyme
Molecule annotation
Chemicals (6 molecules)
* Click molecule labels to explore molecular sequence information.

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