6bdx
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==4-hydroxy tetrahydrodipicolinate reductase from Neisseria gonorrhoeae== | |
| + | <StructureSection load='6bdx' size='340' side='right' caption='[[6bdx]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6bdx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BDX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BDX FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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_reductase 4-hydroxy-tetrahydrodipicolinate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.1.8 1.17.1.8] </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=6bdx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bdx OCA], [http://pdbe.org/6bdx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bdx RCSB], [http://www.ebi.ac.uk/pdbsum/6bdx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bdx ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/A0A1D3EVW8_NEIGO A0A1D3EVW8_NEIGO]] Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.[HAMAP-Rule:MF_00102][SAAS:SAAS00011094] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Neisseria gonorrhoeae, an obligate human pathogen, is a leading cause of communicable diseases globally. Due to rapid development of drug resistance, the rate of successfully curing gonococcal infections is rapidly decreasing. Hence, research is being directed toward finding alternative drugs or drug targets to help eradicate these infections. 4-Hydroxy-tetrahydrodipicolinate reductase (DapB), an important enzyme in the meso-diaminopimelate pathway, is a promising target for the development of new antibiotics. This manuscript describes the first structure of DapB from N. gonorrhoeae determined at 1.85A. This enzyme uses NAD(P)H as cofactor. Details of the interactions of the enzyme with its cofactors and a substrate analog/inhibitor are discussed. A large scale bioinformatics analysis of DapBs' sequences is also described. | ||
| - | + | 4-Hydroxy-tetrahydrodipicolinate reductase from Neisseria gonorrhoeae - structure and interactions with coenzymes and substrate analog.,Pote S, Pye SE, Sheahan TE, Gawlicka-Chruszcz A, Majorek KA, Chruszcz M Biochem Biophys Res Commun. 2018 Aug 6. pii: S0006-291X(18)31651-6. doi:, 10.1016/j.bbrc.2018.07.147. PMID:30093108<ref>PMID:30093108</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 6bdx" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: 4-hydroxy-tetrahydrodipicolinate reductase]] | ||
[[Category: Chruszcz, M]] | [[Category: Chruszcz, M]] | ||
| + | [[Category: Pote, S S]] | ||
| + | [[Category: Pye, S E]] | ||
| + | [[Category: Sheahan, T E]] | ||
| + | [[Category: 4-hydroxy tetrahydrodipicolinate reductase]] | ||
| + | [[Category: Lysine biosynthesis]] | ||
| + | [[Category: Neisseria gonorrhoeae]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 07:25, 29 August 2018
4-hydroxy tetrahydrodipicolinate reductase from Neisseria gonorrhoeae
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