4xky: Difference between revisions
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<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=4xky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xky OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xky RCSB], [http://www.ebi.ac.uk/pdbsum/4xky PDBsum]</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=4xky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xky OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xky RCSB], [http://www.ebi.ac.uk/pdbsum/4xky PDBsum]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Dihydrodipicolinate synthase (DapA) catalyzes the first committed step of the diaminopimelate biosynthetic pathway of lysine. It has been shown to be an essential enzyme in many bacteria and has been the subject of research to generate novel antibiotics. However, this pathway is present in both pathogenic and commensal bacteria, and antibiotics targeting DapA may interfere with normal gut colonization. Bacteroides thetaiotaomicron is a Gram-negative commensal bacterium that makes up a large proportion of the normal microbiota of the human gut. The structure of DapA from B. thetaiotaomicron (BtDapA) has been determined. This structure will help to guide the generation of selectively active antibiotic compounds targeting DapA. | |||
Structure of dihydrodipicolinate synthase from the commensal bacterium Bacteroides thetaiotaomicron at 2.1 A resolution.,Mank N, Arnette A, Klapper V, Offermann L, Chruszcz M Acta Crystallogr F Struct Biol Commun. 2015 Apr;71(Pt 4):449-54. doi:, 10.1107/S2053230X15004628. Epub 2015 Mar 20. PMID:25849508<ref>PMID:25849508</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||
Revision as of 09:52, 22 April 2015
Structure of dihydrodipicolinate synthase from the commensal bacterium Bacteroides thetaiotaomicron at 2.1 A resolutionStructure of dihydrodipicolinate synthase from the commensal bacterium Bacteroides thetaiotaomicron at 2.1 A resolution
Structural highlights
Publication Abstract from PubMedDihydrodipicolinate synthase (DapA) catalyzes the first committed step of the diaminopimelate biosynthetic pathway of lysine. It has been shown to be an essential enzyme in many bacteria and has been the subject of research to generate novel antibiotics. However, this pathway is present in both pathogenic and commensal bacteria, and antibiotics targeting DapA may interfere with normal gut colonization. Bacteroides thetaiotaomicron is a Gram-negative commensal bacterium that makes up a large proportion of the normal microbiota of the human gut. The structure of DapA from B. thetaiotaomicron (BtDapA) has been determined. This structure will help to guide the generation of selectively active antibiotic compounds targeting DapA. Structure of dihydrodipicolinate synthase from the commensal bacterium Bacteroides thetaiotaomicron at 2.1 A resolution.,Mank N, Arnette A, Klapper V, Offermann L, Chruszcz M Acta Crystallogr F Struct Biol Commun. 2015 Apr;71(Pt 4):449-54. doi:, 10.1107/S2053230X15004628. Epub 2015 Mar 20. PMID:25849508[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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