PDBsum entry: 2bkw

Transferase

PDB id: 2bkw

Contents

Protein chain

382 a.a. *

Ligands

GLV

Waters ×89

* Residue conservation analysis

PDB id:

2bkw

Name:

Transferase

Title:

Yeast alanine:glyoxylate aminotransferase yfl030w

Structure:

Alanine-glyoxylate aminotransferase 1. Chain: a. Engineered: yes. Other_details: pyridoxal 5'-phosphate link to a 201, glyoxylate

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Strain: s288c. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Biol. unit:

Dimer (from PDB file)

Resolution:

2.57Å R-factor: 0.198 R-free: 0.258

Authors:

P.Meyer,D.Liger,N.Leulliot,S.Quevillon-Cheruel,C.Z.Zhou, F.Borel,J.L.Ferrer,A.Poupon,J.Janin,H.Van Tilbeurgh

Key ref:

P.Meyer et al. (2005). Crystal structure and confirmation of the alanine:glyoxylate aminotransferase activity of the YFL030w yeast protein. Biochimie, 87, 1041-1047. PubMed id: 16226833 DOI: 10.1016/j.biochi.2005.09.001

Date:

21-Feb-05 Release date: 02-Nov-05

Protein chain

P43567  (AGX1_YEAST) -  Alanine--glyoxylate aminotransferase 1

Seq: 385 a.a.

Struc: 382 a.a.*

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

Enzyme reactions

• Enzyme class: E.C.2.6.1.44 - Alanine--glyoxylate transaminase.
• Reaction: L-alanine + glyoxylate = pyruvate + glycine

L-alanine + glyoxylate (Bound ligand (Het Group name = GLV) corresponds exactly) = pyruvate + glycine

• Cofactor: Pyridoxal 5'-phosphate

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

 Gene Ontology (GO) functional annotation 

• Cellular component: mitochondrion (1 term)
• Biological process: metabolic process (2 terms)
• Biochemical function: catalytic activity (5 terms)

reference

DOI no: 10.1016/j.biochi.2005.09.001

Biochimie 87:1041-1047 (2005)

PubMed id: 16226833

Crystal structure and confirmation of the alanine:glyoxylate aminotransferase activity of the YFL030w yeast protein.

P.Meyer, D.Liger, N.Leulliot, S.Quevillon-Cheruel, C.Z.Zhou, F.Borel, J.L.Ferrer, A.Poupon, J.Janin, H.van Tilbeurgh.

ABSTRACT

We have determined the three-dimensional crystal structure of the protein encoded by the open reading frame YFL030w from Saccharomyces cerevisiae to a resolution of 2.6 A using single wavelength anomalous diffraction. YFL030w is a 385 amino-acid protein with sequence similarity to the aminotransferase family. The structure of the protein reveals a homodimer adopting the fold-type I of pyridoxal 5'-phosphate (PLP)-dependent aminotransferases. The PLP co-factor is covalently bound to the active site in the crystal structure. The protein shows close structural resemblance with the human alanine:glyoxylate aminotransferase (EC 2.6.1.44), an enzyme involved in the hereditary kidney stone disease primary hyperoxaluria type 1. In this paper we show that YFL030w codes for an alanine:glyoxylate aminotransferase, highly specific for its amino donor and acceptor substrates.