3bxy

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[[Image:3bxy.jpg|left|200px]]<br /><applet load="3bxy" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="3bxy, resolution 2.00&Aring;" />
 
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'''Crystal structure of tetrahydrodipicolinate N-succinyltransferase from E. coli'''<br />
 
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==About this Structure==
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==Crystal structure of tetrahydrodipicolinate N-succinyltransferase from E. coli==
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3BXY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BXY OCA].
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<StructureSection load='3bxy' size='340' side='right'caption='[[3bxy]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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[[Category: 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase]]
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== Structural highlights ==
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[[Category: Escherichia coli]]
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<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>
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[[Category: Single protein]]
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</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&#8491;</td></tr>
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[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]]
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<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>
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[[Category: Gehring, K.]]
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</table>
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[[Category: Kozlov, G.]]
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== Function ==
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[[Category: acyltransferase]]
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[https://www.uniprot.org/uniprot/DAPD_ECO57 DAPD_ECO57]
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[[Category: amino-acid biosynthesis]]
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== Evolutionary Conservation ==
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[[Category: bsgi]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: canadian institutes of health research]]
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Check<jmol>
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[[Category: cihr]]
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<jmolCheckbox>
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[[Category: cytoplasm]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bx/3bxy_consurf.spt"</scriptWhenChecked>
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[[Category: diaminopimelate biosynthesis]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: left-handed beta-helix]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: lysine biosynthesis]]
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</jmolCheckbox>
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[[Category: montreal-kingston bacterial structural genomics initiative]]
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</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].
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[[Category: structural genomics]]
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<div style="clear:both"></div>
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[[Category: transferase]]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:07:45 2008''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3bxy" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli O157:H7]]
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[[Category: Large Structures]]
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[[Category: Gehring K]]
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[[Category: Kozlov G]]

Current revision

Crystal structure of tetrahydrodipicolinate N-succinyltransferase from E. coli

PDB ID 3bxy

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