2qf4
From Proteopedia
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|PDB= 2qf4 |SIZE=350|CAPTION= <scene name='initialview01'>2qf4</scene>, resolution 1.200Å | |PDB= 2qf4 |SIZE=350|CAPTION= <scene name='initialview01'>2qf4</scene>, resolution 1.200Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= mreC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=171101 Streptococcus pneumoniae R6]) | |GENE= mreC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=171101 Streptococcus pneumoniae R6]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2qf5|2QF5]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qf4 OCA], [http://www.ebi.ac.uk/pdbsum/2qf4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qf4 RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Lovering, A L.]] | [[Category: Lovering, A L.]] | ||
[[Category: Strynadka, N C.J.]] | [[Category: Strynadka, N C.J.]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: SO4]] | ||
[[Category: filament a-lytic protease fold]] | [[Category: filament a-lytic protease fold]] | ||
[[Category: structural protein]] | [[Category: structural protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:48:33 2008'' |
Revision as of 01:48, 31 March 2008
| |||||||
| , resolution 1.200Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | mreC (Streptococcus pneumoniae R6) | ||||||
| Related: | 2QF5
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
High resolution structure of the major periplasmic domain from the cell shape-determining filament MreC (orthorhombic form)
Overview
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 Structure
2QF4 is a Single protein structure of sequence from Streptococcus pneumoniae r6. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Mar 31 04:48:33 2008
