3bxy
From Proteopedia
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- | [[Image:3bxy.jpg|left|200px]] | ||
- | + | ==Crystal structure of tetrahydrodipicolinate N-succinyltransferase from E. coli== | |
- | + | <StructureSection load='3bxy' size='340' side='right'caption='[[3bxy]], [[Resolution|resolution]] 2.00Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[3bxy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BXY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BXY 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]] 2Å</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=3bxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bxy OCA], [https://pdbe.org/3bxy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bxy RCSB], [https://www.ebi.ac.uk/pdbsum/3bxy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bxy ProSAT]</span></td></tr> |
- | + | </table> | |
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/DAPD_ECO57 DAPD_ECO57] | ||
+ | == 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/bx/3bxy_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=3bxy ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Tetrahydrodipicolinate N-succinyltransferase is an enzyme present in many bacteria that catalyzes the first step of the succinylase pathway for the synthesis of meso-diaminopimelate and the amino acid L-lysine. Inhibition of the synthesis of meso-diaminopimelate, a component of peptidoglycan present in the cell wall of bacteria, is a potential route for the development of novel anti-bacterial agents. Here, we report the crystal structure of the DapD tetrahydrodipicolinate N-succinyltransferase from Escherichia coli at 2.0 A resolution. Comparison of the structure with the homologous enzyme from Mycobacterium bovis reveals the C-terminal helix undergoes a large rearrangement upon substrate binding, which contributes to cooperativity in substrate binding. | ||
- | + | Structure of Escherichia coli tetrahydrodipicolinate N-succinyltransferase reveals the role of a conserved C-terminal helix in cooperative substrate binding.,Nguyen L, Kozlov G, Gehring K FEBS Lett. 2008 Mar 5;582(5):623-6. Epub 2008 Jan 31. PMID:18242192<ref>PMID:18242192</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 3bxy" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | [[Category: Escherichia coli | + | <references/> |
- | + | __TOC__ | |
- | [[Category: | + | </StructureSection> |
- | [[Category: Gehring | + | [[Category: Escherichia coli O157:H7]] |
- | [[Category: Kozlov | + | [[Category: Large Structures]] |
- | + | [[Category: Gehring K]] | |
- | + | [[Category: Kozlov G]] | |
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Current revision
Crystal structure of tetrahydrodipicolinate N-succinyltransferase from E. coli
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