PDBsum entry 4dfe

Transferase

PDB id: 4dfe

Contents

Protein chains

322 a.a.

Ligands

EDO

Waters ×290

PDB id:

4dfe

Name:

Transferase

Title:

Crystal structure of 3-oxoacyl-[acyl-carrier-protein] synthase iii from burkholderia xenovorans

Structure:

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

Source:

Burkholderia xenovorans. Organism_taxid: 266265. Strain: lb400. Gene: fabh, bxeno_a3336, bxe_a1072. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.35Å R-factor: 0.229 R-free: 0.275

Authors:

Seattle Structural Genomics Center For Infectious Disease (Ssgcid)

Key ref:

L.Baugh et al. (2013). Combining functional and structural genomics to sample the essential Burkholderia structome. Plos One, 8, e53851. PubMed id: 23382856

Date:

23-Jan-12 Release date: 08-Feb-12

Protein chains

Q13VL5  (Q13VL5_PARXL) -  Beta-ketoacyl-[acyl-carrier-protein] synthase III from Paraburkholderia xenovorans (strain LB400)

Seq: 329 a.a.

Struc: 322 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

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

malonyl-[ACP] + acetyl-CoA + H(+) = 3-oxobutanoyl-[ACP] + CO2 (Bound ligand (Het Group name = EDO) matches with 40.00% similarity) + CoA

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

reference

Plos One 8:e53851 (2013)

PubMed id: 23382856

Combining functional and structural genomics to sample the essential Burkholderia structome.

L.Baugh, L.A.Gallagher, R.Patrapuvich, M.C.Clifton, A.S.Gardberg, T.E.Edwards, B.Armour, D.W.Begley, S.H.Dieterich, D.M.Dranow, J.Abendroth, J.W.Fairman, D.Fox, B.L.Staker, I.Phan, A.Gillespie, R.Choi, S.Nakazawa-Hewitt, M.T.Nguyen, A.Napuli, L.Barrett, G.W.Buchko, R.Stacy, P.J.Myler, L.J.Stewart, C.Manoil, W.C.Van Voorhis.

ABSTRACT

No abstract given.