PDBsum entry 5cdy

Oxidoreductase

PDB id: 5cdy

Contents

Protein chains

213 a.a.

Ligands

PO4

GOL ×2

Waters ×13

PDB id:

5cdy

Name:

Oxidoreductase

Title:

The crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase (fabg) from yersinia pestis at 2.85a resolution

Structure:

3-oxoacyl-[acyl-carrier protein] reductase. Chain: a, b, c, d. Synonym: 3-oxoacyl-[acyl-carrier-protein] reductase. Engineered: yes

Source:

Yersinia pestis. Organism_taxid: 632. Gene: fabg, y1758, ypo1599. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.85Å R-factor: 0.214 R-free: 0.246

Authors:

J.D.Nanson,J.K.Forwood

Key ref:

J.D.Nanson and J.K.Forwood (2015). Structural Characterisation of FabG from Yersinia pestis, a Key Component of Bacterial Fatty Acid Synthesis. Plos One, 10, e0141543. PubMed id: 26539719 DOI: 10.1371/journal.pone.0141543

Date:

06-Jul-15 Release date: 18-Nov-15

Protein chains

A0A5P8YI04  (A0A5P8YI04_YERPE) -  3-oxoacyl-[acyl-carrier-protein] reductase from Yersinia pestis

Seq: 244 a.a.

Struc: 213 a.a.

Enzyme reactions

• Enzyme class: E.C.1.1.1.100 - 3-oxoacyl-[acyl-carrier-protein] reductase.
• Reaction: a (3R)-hydroxyacyl-[ACP] + NADP⁺ = a 3-oxoacyl-[ACP] + NADPH + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1371/journal.pone.0141543

Plos One 10:e0141543 (2015)

PubMed id: 26539719

Structural Characterisation of FabG from Yersinia pestis, a Key Component of Bacterial Fatty Acid Synthesis.

J.D.Nanson, J.K.Forwood.

ABSTRACT

Ketoacyl-acyl carrier protein reductases (FabG) are ubiquitously expressed enzymes that catalyse the reduction of acyl carrier protein (ACP) linked thioesters within the bacterial type II fatty acid synthesis (FASII) pathway. The products of these enzymes, saturated and unsaturated fatty acids, are essential components of the bacterial cell envelope. The FASII reductase enoyl-ACP reductase (FabI) has been the focus of numerous drug discovery efforts, some of which have led to clinical trials, yet few studies have focused on FabG. Like FabI, FabG appears to be essential for survival in many bacteria, similarly indicating the potential of this enzyme as a drug target. FabG enzymes are members of the short-chain alcohol dehydrogenase/reductase (SDR) family, and like other SDRs, exhibit highly conserved secondary and tertiary structures, and contain a number of conserved sequence motifs. Here we describe the crystal structures of FabG from Yersinia pestis (YpFabG), the causative agent of bubonic, pneumonic, and septicaemic plague, and three human pandemics. Y. pestis remains endemic in many parts of North America, South America, Southeast Asia, and Africa, and a threat to human health. YpFabG shares a high degree of structural similarity with bacterial homologues, and the ketoreductase domain of the mammalian fatty acid synthase from both Homo sapiens and Sus scrofa. Structural characterisation of YpFabG, and comparison with other bacterial FabGs and the mammalian fatty acid synthase, provides a strong platform for virtual screening of potential inhibitors, rational drug design, and the development of new antimicrobial agents to combat Y. pestis infections.