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3ne8
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:3ne8.jpg|left|200px]] | ||
| - | < | + | ==The crystal structure of a domain from N-acetylmuramoyl-l-alanine amidase of Bartonella henselae str. Houston-1== |
| - | + | <StructureSection load='3ne8' size='340' side='right' caption='[[3ne8]], [[Resolution|resolution]] 1.24Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[3ne8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_49882 Atcc 49882]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NE8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NE8 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | - | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">amiB, BH08710 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=38323 ATCC 49882])</td></tr> | |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ne8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ne8 OCA], [http://pdbe.org/3ne8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ne8 RCSB], [http://www.ebi.ac.uk/pdbsum/3ne8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ne8 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/ne/3ne8_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=3ne8 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Remodelling of the peptidoglycan (PG) exoskeleton is intimately tied to the growth and division of bacteria. Enzymes that hydrolyse PG are critical for these processes, but their activities must be tightly regulated to prevent the generation of lethal breaches in the PG matrix. Despite their importance, the mechanisms regulating PG hydrolase activity have remained elusive. Here we investigate the control of cell division hydrolases called amidases (AmiA, AmiB and AmiC) required for Escherichia coli cell division. Poorly regulated amiB mutants were isolated encoding lytic AmiB variants with elevated basal PG hydrolase activities in vitro. The structure of an AmiB orthologue was also solved, revealing that the active site of AmiB is occluded by a conserved alpha helix. Strikingly, most of the amino acid substitutions in the lytic AmiB variants mapped to this domain and are predicted to disrupt its interaction with the active site. Our results therefore support a model in which cell separation is stimulated by the reversible relief of amidase autoinhibition governed by conserved subcomplexes within the cytokinetic ring. Analogous conformational control mechanisms are likely to be part of a general strategy used to control PG hydrolases present within multienzyme PG-remodelling machines. | ||
| - | + | A conformational switch controls cell wall-remodelling enzymes required for bacterial cell division.,Yang DC, Tan K, Joachimiak A, Bernhardt TG Mol Microbiol. 2012 Aug;85(4):768-81. doi: 10.1111/j.1365-2958.2012.08138.x. Epub, 2012 Jul 11. PMID:22715947<ref>PMID:22715947</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3ne8" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| - | [[Category: Buck, K | + | <references/> |
| - | [[Category: Joachimiak, A | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: Rakowski, E | + | [[Category: Atcc 49882]] |
| - | [[Category: Tan, K | + | [[Category: Buck, K]] |
| + | [[Category: Joachimiak, A]] | ||
| + | [[Category: Structural genomic]] | ||
| + | [[Category: Rakowski, E]] | ||
| + | [[Category: Tan, K]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Mcsg]] | [[Category: Mcsg]] | ||
| - | [[Category: | + | [[Category: PSI, Protein structure initiative]] |
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Current revision
The crystal structure of a domain from N-acetylmuramoyl-l-alanine amidase of Bartonella henselae str. Houston-1
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