PDBsum entry 4hl6

Transferase

PDB id: 4hl6

Contents

Protein chains

(+ 0 more) 375 a.a.

Waters ×1021

PDB id:

4hl6

Name:

Transferase

Title:

Yfde from escherichia coli

Structure:

Uncharacterized protein yfde. Chain: a, b, c, d, e, f. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: yfde, b2371, jw2368. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.12Å R-factor: 0.191 R-free: 0.236

Authors:

E.A.Mullins,K.L.Sullivan,K.E.Nyffeler,T.J.Kappock

Key ref:

E.A.Mullins et al. (2013). Function and X-ray crystal structure of Escherichia coli YfdE. Plos One, 8, e67901. PubMed id: 23935849 DOI: 10.1371/journal.pone.0067901

Date:

16-Oct-12 Release date: 22-May-13

Protein chains

P76518  (ACOCT_ECOLI) -  Acetyl-CoA:oxalate CoA-transferase from Escherichia coli (strain K12)

Seq: 381 a.a.

Struc: 375 a.a.

Enzyme reactions

• Enzyme class: E.C.2.8.3.19 - CoA:oxalate CoA-transferase.
• Reaction: oxalate + acetyl-CoA = oxalyl-CoA + acetate

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

reference

DOI no: 10.1371/journal.pone.0067901

Plos One 8:e67901 (2013)

PubMed id: 23935849

Function and X-ray crystal structure of Escherichia coli YfdE.

E.A.Mullins, K.L.Sullivan, T.J.Kappock.

ABSTRACT

Many food plants accumulate oxalate, which humans absorb but do not metabolize, leading to the formation of urinary stones. The commensal bacterium Oxalobacter formigenes consumes oxalate by converting it to oxalyl-CoA, which is decarboxylated by oxalyl-CoA decarboxylase (OXC). OXC and the class III CoA-transferase formyl-CoA:oxalate CoA-transferase (FCOCT) are widespread among bacteria, including many that have no apparent ability to degrade or to resist external oxalate. The EvgA acid response regulator activates transcription of the Escherichia coli yfdXWUVE operon encoding YfdW (FCOCT), YfdU (OXC), and YfdE, a class III CoA-transferase that is [Formula: see text]30% identical to YfdW. YfdW and YfdU are necessary and sufficient for oxalate-induced protection against a subsequent acid challenge; neither of the other genes has a known function. We report the purification, in vitro characterization, 2.1-Å crystal structure, and functional assignment of YfdE. YfdE and UctC, an orthologue from the obligate aerobe Acetobacter aceti, perform the reversible conversion of acetyl-CoA and oxalate to oxalyl-CoA and acetate. The annotation of YfdE as acetyl-CoA:oxalate CoA-transferase (ACOCT) expands the scope of metabolic pathways linked to oxalate catabolism and the oxalate-induced acid tolerance response. FCOCT and ACOCT active sites contain distinctive, conserved active site loops (the glycine-rich loop and the GNxH loop, respectively) that appear to encode substrate specificity.