4j3d

Pseudomonas aeruginosa LpxC in complex with a hydroxamate inhibitorPseudomonas aeruginosa LpxC in complex with a hydroxamate inhibitor

Structural highlights 4j3d is a 2 chain structure with sequence from Pseudomonas aeruginosa pao1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , Gene: lpxC, envA, PA4406 (Pseudomonas aeruginosa PAO1) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Lipopolysaccharide (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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also UDP-3-O-acyl-N-acetylglucosamine deacetylase

spinqualitylabelsall models 4j3d, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image