PDBsum entry 3ba1

Oxidoreductase

PDB id: 3ba1

Contents

Protein chain

312 a.a. *

Waters ×290

* Residue conservation analysis

PDB id:

3ba1

Name:

Oxidoreductase

Title:

Structure of hydroxyphenylpyruvate reductase from coleus blumei

Structure:

Hydroxyphenylpyruvate reductase. Chain: a. Synonym: hppr. Engineered: yes

Source:

Solenostemon scutellarioides. Coleus blumei. Organism_taxid: 4142. Gene: hppr. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.47Å R-factor: 0.150 R-free: 0.203

Authors:

V.Janiak,G.Klebe,M.Petersen,A.Heine

Key ref:

V.Janiak et al. (2010). Structure and substrate docking of a hydroxy(phenyl)pyruvate reductase from the higher plant Coleus blumei Benth. Acta Crystallogr D Biol Crystallogr, 66, 593-603. PubMed id: 20445235

Date:

07-Nov-07 Release date: 11-Nov-08

Protein chain

Q65CJ7  (HPPR_PLESU) -  Hydroxyphenylpyruvate reductase from Plectranthus scutellarioides

Seq: 313 a.a.

Struc: 312 a.a.

Enzyme reactions

• Enzyme class: E.C.1.1.1.237 - hydroxyphenylpyruvate reductase.
• Reaction:
  1. (2R)-2-hydroxy-3-(4-hydroxyphenyl)propanoate + NADP⁺ = 3-(4-hydroxyphenyl)pyruvate + NADPH + H⁺
  2. (2R)-2-hydroxy-3-(4-hydroxyphenyl)propanoate + NAD⁺ = 3-(4-hydroxyphenyl)pyruvate + NADH + H⁺
  3. (2R)-3-(3,4-dihydroxyphenyl)lactate + NAD⁺ = 3-(3,4- dihydroxyphenyl)pyruvate + NADH + H⁺
  4. (2R)-3-(3,4-dihydroxyphenyl)lactate + NADP⁺ = 3-(3,4- dihydroxyphenyl)pyruvate + NADPH + H⁺

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

reference

Acta Crystallogr D Biol Crystallogr 66:593-603 (2010)

PubMed id: 20445235

Structure and substrate docking of a hydroxy(phenyl)pyruvate reductase from the higher plant Coleus blumei Benth.

V.Janiak, M.Petersen, M.Zentgraf, G.Klebe, A.Heine.

ABSTRACT

Hydroxy(phenyl)pyruvate reductase [H(P)PR] belongs to the family of D-isomer-specific 2-hydroxyacid dehydrogenases and catalyzes the reduction of hydroxyphenylpyruvates as well as hydroxypyruvate and pyruvate to the corresponding lactates. Other non-aromatic substrates are also accepted. NADPH is the preferred cosubstrate. The crystal structure of the enzyme from Coleus blumei (Lamiaceae) has been determined at 1.47 A resolution. In addition to the apoenzyme, the structure of a complex with NADP(+) was determined at a resolution of 2.2 A. H(P)PR is a dimer with a molecular mass of 34 113 Da per subunit. The structure is similar to those of other members of the enzyme family and consists of two domains separated by a deep catalytic cleft. To gain insights into substrate binding, several compounds were docked into the cosubstrate complex structure using the program AutoDock. The results show two possible binding modes with similar docking energy. However, only binding mode A provides the necessary environment in the active centre for hydride and proton transfer during reduction, leading to the formation of the (R)-enantiomer of lactate and/or hydroxyphenyllactate.