6u01: Difference between revisions

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-'''Unreleased structure'''
-The entry 6u01 is ON HOLD  until Paper Publication
+==Dihydrodipicolinate synthase (DHDPS) from C.jejuni, N84D mutant with pyruvate bound in the active site==
+<StructureSection load='6u01' size='340' side='right'caption='[[6u01]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6u01]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U01 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6U01 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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
+<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KPI:(2S)-2-AMINO-6-[(1-HYDROXY-1-OXO-PROPAN-2-YLIDENE)AMINO]HEXANOIC+ACID'>KPI</scene></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxy-tetrahydrodipicolinate_synthase 4-hydroxy-tetrahydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.3.7 4.3.3.7] </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=6u01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u01 OCA], [http://pdbe.org/6u01 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6u01 RCSB], [http://www.ebi.ac.uk/pdbsum/6u01 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6u01 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/A0A2U0QMK8_CAMJU A0A2U0QMK8_CAMJU]] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[HAMAP-Rule:MF_00418][SAAS:SAAS00570606]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Dihydrodipicolinate synthase (DHDPS) from Campylobacter jejuni is a natively homotetrameric enzyme that catalyzes the first unique reaction of (S)-lysine biosynthesis and is feedback-regulated by lysine through binding to an allosteric site. High-resolution structures of the DHDPS-lysine complex have revealed significant insights into the binding events. One key asparagine residue, N84, makes hydrogen bonds with both the carboxyl and the alpha-amino group of the bound lysine. We generated two mutants, N84A and N84D, to study the effects of these changes on the allosteric site properties. However, under normal assay conditions, N84A displayed notably lower catalytic activity, and N84D showed no activity. Here we show that these mutations disrupt the quaternary structure of DHDPS in a concentration-dependent fashion, as demonstrated by size-exclusion chromatography, multi-angle light scattering, dynamic light scattering, small-angle X-ray scattering (SAXS) and high-resolution protein crystallography.
-Authors: Saran, S., Majdi Yazdi, M., Lehnert, L., Palmer, D.R.J., Sanders, D.A.R.
+Asparagine-84, a regulatory allosteric site residue, helps maintain the quaternary structure of Campylobacter jejuni dihydrodipicolinate synthase.,Majdi Yazdi M, Saran S, Mrozowich T, Lehnert C, Patel TR, Sanders DAR, Palmer DRJ J Struct Biol. 2019 Oct 31:107409. doi: 10.1016/j.jsb.2019.107409. PMID:31678256<ref>PMID:31678256</ref>
-Description: Dihydrodipicolinate synthase (DHDPS) from C.jejuni, N84D mutant with pyruvate bound in the active site
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Palmer, D.R.J]]
+<div class="pdbe-citations 6u01" style="background-color:#fffaf0;"></div>
-[[Category: Sanders, D.A.R]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: 4-hydroxy-tetrahydrodipicolinate synthase]]
+[[Category: Large Structures]]
+[[Category: Lehnert, L]]
+[[Category: Palmer, D R.J]]
+[[Category: Sanders, D A.R]]
 [[Category: Saran, S]]
-[[Category: Lehnert, L]]
+[[Category: Yazdi, M Majdi]]
-[[Category: Majdi Yazdi, M]]
+[[Category: Dihydrodipicolinate synthase]]
+[[Category: Lyase]]
+[[Category: Tetrameric protein]]
+[[Category: Tim barrel]]