2qf5
From Proteopedia
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| - | [[Image:2qf5.jpg|left|200px]] | ||
| - | + | ==High resolution structure of the major periplasmic domain from the cell shape-determining filament MreC (monoclinic form)== | |
| - | + | <StructureSection load='2qf5' size='340' side='right'caption='[[2qf5]], [[Resolution|resolution]] 2.23Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2qf5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_R6 Streptococcus pneumoniae R6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QF5 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.23Å</td></tr> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qf5 OCA], [https://pdbe.org/2qf5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qf5 RCSB], [https://www.ebi.ac.uk/pdbsum/2qf5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qf5 ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/MREC_STRR6 MREC_STRR6] Involved in formation and maintenance of cell shape.[UniProtKB:Q01466] | |
| - | + | == Evolutionary Conservation == | |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | == | + | Check<jmol> |
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qf/2qf5_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qf5 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
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. | 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. | ||
| - | + | 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<ref>PMID:17707860</ref> | |
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| - | High-resolution structure of the major periplasmic domain from the cell shape-determining filament MreC., Lovering AL, Strynadka NC | + | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2qf5" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptococcus pneumoniae R6]] | ||
| + | [[Category: Lovering AL]] | ||
| + | [[Category: Strynadka NCJ]] | ||
Current revision
High resolution structure of the major periplasmic domain from the cell shape-determining filament MreC (monoclinic form)
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