PDBsum entry 3ps2

Hydrolase/antibiotic

PDB id: 3ps2

Contents

Protein chain

300 a.a. *

Ligands

ZH4

UKW

DMS ×3

SO4 ×3

Metals

_ZN

Waters ×105

* Residue conservation analysis

PDB id:

3ps2

Name:

Hydrolase/antibiotic

Title:

Crystal structure of the escherichia coli lpxc/lpc-012 complex

Structure:

Udp-3-o-[3-hydroxymyristoyl] n-acetylglucosamine deacetylase. Chain: a. Fragment: unp residues 1-300. Synonym: udp-3-o-acyl-glcnac deacetylase. Engineered: yes

Source:

Escherichia coli ihe3034. Organism_taxid: 714962. Strain: ihe3034 / expec. Gene: ecok1_0097, enva, lpxc. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.30Å R-factor: 0.210 R-free: 0.261

Authors:

C.-J.Lee,P.Zhou

Key ref:

X.Liang et al. (2011). Syntheses, structures and antibiotic activities of LpxC inhibitors based on the diacetylene scaffold. Bioorg Med Chem Lett, 19, 852-860. PubMed id: 21194954

Date:

30-Nov-10 Release date: 19-Jan-11

Protein chain

D5CV28  (D5CV28_ECOKI) -

Enzyme reactions

• Enzyme class: E.C.3.5.1.- - ?????

Bioorg Med Chem Lett 19:852-860 (2011)

PubMed id: 21194954

Syntheses, structures and antibiotic activities of LpxC inhibitors based on the diacetylene scaffold.

X.Liang, C.J.Lee, X.Chen, H.S.Chung, D.Zeng, C.R.Raetz, Y.Li, P.Zhou, E.J.Toone.

ABSTRACT

Compounds inhibiting LpxC in the lipid A biosynthetic pathway are promising leads for novel antibiotics against multidrug-resistant Gram-negative pathogens. We report the syntheses and structural and biochemical characterizations of LpxC inhibitors based on a diphenyl-diacetylene (1,4-diphenyl-1,3-butadiyne) threonyl-hydroxamate scaffold. These studies provide a molecular interpretation for the differential antibiotic activities of compounds with a substituted distal phenyl ring as well as the absolute stereochemical requirement at the C2, but not C3, position of the threonyl group.