4j3d: 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=4j3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j3d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j3d RCSB], [http://www.ebi.ac.uk/pdbsum/4j3d 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=4j3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j3d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j3d RCSB], [http://www.ebi.ac.uk/pdbsum/4j3d PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/LPXC_PSEAE LPXC_PSEAE]] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | |||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 21:51, 24 December 2014
Pseudomonas aeruginosa LpxC in complex with a hydroxamate inhibitorPseudomonas aeruginosa LpxC in complex with a hydroxamate inhibitor
Structural highlights
Function[LPXC_PSEAE] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. Publication Abstract from PubMedLipopolysaccharide (LPS) biosynthesis is an attractive antibacterial target as it is both conserved and essential for the survival of key pathogenic bacteria. Lipid A is the hydrophobic anchor for LPS and a key structural component of the outer membrane of Gram-negative bacteria. Lipid A biosynthesis is performed in part by a unique zinc dependent metalloamidase, LpxC (UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase), which catalyzes the first non-reversible step in lipid A biosynthesis. The UDP portion of the LpxC substrate-binding pocket has been relatively unexplored. We have designed and evaluated a series of hydroxamate based inhibitors which explore the SAR of substitutions directed into the UDP pocket with a range of substituted alpha-amino acid based linkers. We also provide the first wild type structure of Pseudomonas aeruginosa LpxC which was utilized in the design of many of these analogs. Exploring the UDP pocket of LpxC through amino acid analogs.,Hale MR, Hill P, Lahiri S, Miller MD, Ross P, Alm R, Gao N, Kutschke A, Johnstone M, Prince B, Thresher J, Yang W Bioorg Med Chem Lett. 2013 Apr 15;23(8):2362-7. doi: 10.1016/j.bmcl.2013.02.055. , Epub 2013 Mar 1. PMID:23499237[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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