Download MendeleyHigh-resolution Structure of the Major Periplasmic Domain from the Cell Shape-determining Filament MreC.
Lovering, A.L., Strynadka, N.C.(2007) J Mol Biology 372: 1034-1044
- PubMed: 17707860
- DOI: https://doi.org/10.1016/j.jmb.2007.07.022
- Primary Citation of Related Structures:
2QF4, 2QF5 - PubMed Abstract:
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.
- Department of Biochemistry and Molecular Biology and Center for Blood Research, The University of British Columbia, Vancouver, Canada V6T 1R9.
Organizational Affiliation:
