3bxy
From Proteopedia
(Difference between revisions)
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- | + | ==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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BXY FirstGlance]. <br> | ||
+ | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tdt|1tdt]], [[2tdt|2tdt]], [[3tdt|3tdt]], [[1kgq|1kgq]], [[1kgt|1kgt]]</td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dapD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 Escherichia coli O157:H7])</td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2,3,4,5-tetrahydropyridine-2,6-dicarboxylate_N-succinyltransferase 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.117 2.3.1.117] </span></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=3bxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bxy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3bxy RCSB], [http://www.ebi.ac.uk/pdbsum/3bxy PDBsum]</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/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/chain_selection.php?pdb_ID=2ata 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> | |
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase]] | [[Category: 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase]] | ||
[[Category: Escherichia coli o157:h7]] | [[Category: Escherichia coli o157:h7]] |
Revision as of 06:50, 10 October 2014
Crystal structure of tetrahydrodipicolinate N-succinyltransferase from E. coli
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Categories: 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase | Escherichia coli o157:h7 | BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative. | Gehring, K. | Kozlov, G. | Acyltransferase | Amino-acid biosynthesis | Bsgi | Canadian institutes of health research | Cihr | Diaminopimelate biosynthesis | Left-handed beta-helix | Lysine biosynthesis | Montreal-kingston bacterial structural genomics initiative | Structural genomic | Transferase