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==Crystal Structure of Dihydrodipicolinate synthase from Staphylococcus aureus== | ==Crystal Structure of Dihydrodipicolinate synthase from Staphylococcus aureus== | ||
<StructureSection load='3di0' size='340' side='right' caption='[[3di0]], [[Resolution|resolution]] 2.38Å' scene=''> | <StructureSection load='3di0' size='340' side='right'caption='[[3di0]], [[Resolution|resolution]] 2.38Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3di0]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3di0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_COL Staphylococcus aureus subsp. aureus COL]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DI0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DI0 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.38Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3di0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3di0 OCA], [https://pdbe.org/3di0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3di0 RCSB], [https://www.ebi.ac.uk/pdbsum/3di0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3di0 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/DAPA_STAAC DAPA_STAAC] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).<ref>PMID:18671976</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 38: | Line 36: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Staphylococcus aureus subsp. aureus COL]] | ||
[[Category: Tavarekere | [[Category: Tavarekere GS]] | ||
Latest revision as of 18:09, 1 November 2023
Crystal Structure of Dihydrodipicolinate synthase from Staphylococcus aureusCrystal Structure of Dihydrodipicolinate synthase from Staphylococcus aureus
Structural highlights
FunctionDAPA_STAAC Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedLysine biosynthesis is crucial for cell-wall formation in bacteria. Enzymes involved in lysine biosynthesis are thus potential targets for anti-microbial therapeutics. Dihydrodipicolinate synthase (DHDPS) catalyzes the first step of this pathway. Unlike its homologues, Staphylococcus aureus DHDPS is a dimer both in solution and in the crystal and is not feedback inhibited by lysine. The crystal structure of S. aureus DHDPS in the free and substrate bound forms provides a structural rationale for its catalytic mechanism. The structure also reveals unique conformational features of the S. aureus enzyme that could be crucial for the design of specific non-competitive inhibitors. Structural and functional characterization of Staphylococcus aureus dihydrodipicolinate synthase.,Girish TS, Sharma E, Gopal B FEBS Lett. 2008 Aug 20;582(19):2923-30. Epub 2008 Jul 29. PMID:18671976[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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