PDBsum entry 1vpd

Oxidoreductase

PDB id: 1vpd

Contents

Protein chain

294 a.a. *

Ligands

TLA

Metals

_CL

Waters ×497

* Residue conservation analysis

PDB id:

1vpd

Name:

Oxidoreductase

Title:

X-ray crystal structure of tartronate semialdehyde reductase [salmonella typhimurium lt2]

Structure:

Tartronate semialdehyde reductase. Chain: a. Engineered: yes

Source:

Salmonella typhimurium. Organism_taxid: 602. Gene: garr. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Tetramer (from PQS)

Resolution:

1.65Å R-factor: 0.121 R-free: 0.144

Authors:

J.Osipiuk,M.Zhou,S.Moy,F.Collart,A.Joachimiak,Midwest Center For Structural Genomics (Mcsg)

Key ref:

J.Osipiuk et al. (2009). X-ray crystal structure of GarR-tartronate semialdehyde reductase from Salmonella typhimurium. J Struct Funct Genomics, 10, 249-253. PubMed id: 19184529

Date:

22-Oct-04 Release date: 26-Oct-04

Supersedes:

1tea

Protein chain

Q8ZLV8  (Q8ZLV8_SALTY) -  2-hydroxy-3-oxopropionate reductase from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

Seq: 296 a.a.

Struc: 294 a.a.

Enzyme reactions

• Enzyme class: E.C.1.1.1.60 - 2-hydroxy-3-oxopropionate reductase.
• Reaction:
  1. (R)-glycerate + NADP⁺ = 2-hydroxy-3-oxopropanoate + NADPH + H⁺
  2. (R)-glycerate + NAD⁺ = 2-hydroxy-3-oxopropanoate + NADH + H⁺

(R)-glycerate (Bound ligand (Het Group name = TLA) matches with 70.00% similarity) + NADP(+) = 2-hydroxy-3-oxopropanoate + NADPH + H(+)

(R)-glycerate (Bound ligand (Het Group name = TLA) matches with 70.00% similarity) + NAD(+) = 2-hydroxy-3-oxopropanoate + NADH + H(+)

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

reference

J Struct Funct Genomics 10:249-253 (2009)

PubMed id: 19184529

X-ray crystal structure of GarR-tartronate semialdehyde reductase from Salmonella typhimurium.

J.Osipiuk, M.Zhou, S.Moy, F.Collart, A.Joachimiak.

ABSTRACT

Tartronate semialdehyde reductases (TSRs), also known as 2-hydroxy-3-oxopropionate reductases, catalyze the reduction of tartronate semialdehyde using NAD as cofactor in the final stage of D-glycerate biosynthesis. These enzymes belong to family of structurally and mechanically related beta-hydroxyacid dehydrogenases which differ in substrate specificity and catalyze reactions in specific metabolic pathways. Here, we present the crystal structure of GarR a TSR from Salmonella typhimurium determined by the single-wavelength anomalous diffraction method and refined to 1.65 A resolution. The active site of the enzyme contains L-tartrate which most likely mimics a position of a glycerate which is a product of the enzyme reaction. The analysis of the TSR structure shows also a putative NADPH binding site in the enzyme.