2QF4

High resolution structure of the major periplasmic domain from the cell shape-determining filament MreC (orthorhombic form)

Summary for 2QF4

• Entry DOI: 10.2210/pdb2qf4/pdb
• Related: 2QF5
• Descriptor: Cell shape determining protein MreC, 1,2-ETHANEDIOL, SULFATE ION, ... (4 entities in total)
• Functional Keywords: filament a-lytic protease fold, structural protein
• Biological source: Streptococcus pneumoniae
• Total number of polymer chains: 2
• Total formula weight: 36737.18

Authors

Lovering, A.L.,Strynadka, N.C.J. (deposition date: 2007-06-26, release date: 2007-08-07, Last modification date: 2024-02-21)

Primary citation

Lovering, A.L.,Strynadka, N.C.
High-resolution Structure of the Major Periplasmic Domain from the Cell Shape-determining Filament MreC.
J.Mol.Biol., 372:1034-1044, 2007

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.

PubMed: 17707860
DOI: 10.1016/j.jmb.2007.07.022

Experimental method

X-RAY DIFFRACTION (1.2 Å)