2qf4
High resolution structure of the major periplasmic domain from the cell shape-determining filament MreC (orthorhombic form)
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OverviewOverview
Bacterial cell shape is dictated by the cell wall, a plastic structure, that must adapt to growth and division whilst retaining its function as a, selectively permeable barrier. The modulation of cell wall structure is, achieved by a variety of enzymatic functions, all of which must be, spatially regulated in a precise manner. The membrane-spanning essential, protein MreC has been identified as the central hub in this process, linking the bacterial cytoskeleton to a variety of cell wall-modifying, enzymes. Additionally, MreC can form filaments, believed to run, perpendicularly to the membrane. We present here the 1.2 A resolution, crystal structure of the major periplasmic domain of Streptococcus, pneumoniae MreC. The protein shows a novel arrangement of two, barrel-shaped domains, one of which shows homology to a known protein, oligomerization motif, with the other resembling a catalytic domain from a, bacterial protease. We discuss the implications of these results for MreC, function, and detail the structural features of the molecule that may be, responsible for the binding of partner proteins.
About this StructureAbout this Structure
2QF4 is a Single protein structure of sequence from Streptococcus pneumoniae r6 with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
High-resolution Structure of the Major Periplasmic Domain from the Cell Shape-determining Filament MreC., Lovering AL, Strynadka NC, J Mol Biol. 2007 Sep 28;372(4):1034-44. Epub 2007 Jul 26. PMID:17707860
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