PDBsum entry 4z19

Transferase

PDB id: 4z19

Contents

Protein chain

309 a.a.

Ligands

GOL ×2

Waters ×230

PDB id:

4z19

Name:

Transferase

Title:

Crystal structure of beta-ketoacyl-acp synthase iii (fabh) from yersinia pestis with acetylated active site cysteine

Structure:

3-oxoacyl-[acyl-carrier-protein] synthase 3. Chain: a. Synonym: 3-oxoacyl-[acyl-carrier-protein] synthase iii,beta-ketoacyl- acp synthase iii,kas iii. Engineered: yes. Mutation: yes

Source:

Yersinia pestis. Organism_taxid: 632. Gene: fabh, ypo1597, y1756, yp_2257. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.80Å R-factor: 0.149 R-free: 0.179

Authors:

J.D.Nanson,J.K.Forwood

Key ref:

J.D.Nanson et al. (2015). Structural Characterisation of the Beta-Ketoacyl-Acyl Carrier Protein Synthases, FabF and FabH, of Yersinia pestis. Sci Rep, 5, 14797. PubMed id: 26469877 DOI: 10.1038/srep14797

Date:

27-Mar-15 Release date: 20-May-15

Protein chain

Q8ZFT7  (FABH_YERPE) -  Beta-ketoacyl-[acyl-carrier-protein] synthase III from Yersinia pestis

Seq: 316 a.a.

Struc: 309 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.2.3.1.180 - beta-ketoacyl-[acyl-carrier-protein] synthase Iii.
• Reaction: malonyl-[ACP] + acetyl-CoA + H⁺ = 3-oxobutanoyl-[ACP] + CO2 + CoA

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

reference

DOI no: 10.1038/srep14797

Sci Rep 5:14797 (2015)

PubMed id: 26469877

Structural Characterisation of the Beta-Ketoacyl-Acyl Carrier Protein Synthases, FabF and FabH, of Yersinia pestis.

J.D.Nanson, Z.Himiari, C.M.Swarbrick, J.K.Forwood.

ABSTRACT

Yersinia pestis, the causative agent of bubonic, pneumonic, and septicaemic plague, remains a major public health threat, with outbreaks of disease occurring in China, Madagascar, and Peru in the last five years. The existence of multidrug resistant Y. pestis and the potential of this bacterium as a bioterrorism agent illustrates the need for new antimicrobials. The β-ketoacyl-acyl carrier protein synthases, FabB, FabF, and FabH, catalyse the elongation of fatty acids as part of the type II fatty acid biosynthesis (FASII) system, to synthesise components of lipoproteins, phospholipids, and lipopolysaccharides essential for bacterial growth and survival. As such, these enzymes are promising targets for the development of novel therapeutic agents. We have determined the crystal structures of the Y. pestis β-ketoacyl-acyl carrier protein synthases FabF and FabH, and compared these with the unpublished, deposited structure of Y. pestis FabB. Comparison of FabB, FabF, and FabH provides insights into the substrate specificities of these enzymes, and investigation of possible interactions with known β-ketoacyl-acyl carrier protein synthase inhibitors suggests FabB, FabF and FabH may be targeted simultaneously to prevent synthesis of the fatty acids necessary for growth and survival.