PDBsum entry 3hdh

Oxidoreductase

PDB id: 3hdh

Contents

Protein chains

291 a.a. *

265 a.a. *

Ligands

NAD ×3

Waters ×23

* Residue conservation analysis

PDB id:

3hdh

Name:

Oxidoreductase

Title:

Pig heart short chain l-3-hydroxyacyl coa dehydrogenase revisited: sequence analysis and crystal structure determination

Structure:

Protein (l-3-hydroxyacyl coa dehydrogenase). Chain: a, b, c. Synonym: schad. Ec: 1.1.1.35

Source:

Sus scrofa. Pig. Organism_taxid: 9823. Organ: heart. Organelle: mitochondrial

Biol. unit:

Dimer (from PDB file)

Resolution:

2.80Å R-factor: 0.223 R-free: 0.287

Authors:

J.J.Barycki,L.K.O'Brien,J.J.Birktoft,A.W.Strauss,L.J.Banaszak

Key ref:

J.J.Barycki et al. (1999). Pig heart short chain L-3-hydroxyacyl-CoA dehydrogenase revisited: sequence analysis and crystal structure determination. Protein Sci, 8, 2010-2018. PubMed id: 10548046 DOI: 10.1110/ps.8.10.2010

Date:

13-Apr-99 Release date: 08-Oct-99

Protein chains

P00348  (HCDH_PIG) -  Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial from Sus scrofa

Seq: 314 a.a.

Struc: 291 a.a.

Protein chain

P00348  (HCDH_PIG) -  Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial from Sus scrofa

Seq: 314 a.a.

Struc: 265 a.a.

Enzyme reactions

• Enzyme class: Chains A, B, C: E.C.1.1.1.35 - 3-hydroxyacyl-CoA dehydrogenase.
• Reaction: a (3S)-3-hydroxyacyl-CoA + NAD⁺ = a 3-oxoacyl-CoA + NADH + H⁺

(3S)-3-hydroxyacyl-CoA + NAD(+) (Bound ligand (Het Group name = NAD) corresponds exactly) = 3-oxoacyl-CoA + NADH + H(+)

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

reference

DOI no: 10.1110/ps.8.10.2010

Protein Sci 8:2010-2018 (1999)

PubMed id: 10548046

Pig heart short chain L-3-hydroxyacyl-CoA dehydrogenase revisited: sequence analysis and crystal structure determination.

J.J.Barycki, L.K.O'Brien, J.J.Birktoft, A.W.Strauss, L.J.Banaszak.

ABSTRACT

Short chain L-3-hydroxyacyl CoA dehydrogenase (SCHAD) is a soluble dimeric enzyme critical for oxidative metabolism of fatty acids. Its primary sequence has been reported to be conserved across numerous tissues and species with the notable exception of the pig heart homologue. Preliminary efforts to solve the crystal structure of the dimeric pig heart SCHAD suggested the unprecedented occurrence of three enzyme subunits within the asymmetric unit, a phenomenon that was thought to have hampered refinement of the initial chain tracing. The recently solved crystal coordinates of human heart SCHAD facilitated a molecular replacement solution to the pig heart SCHAD data. Refinement of the model, in conjunction with the nucleotide sequence for pig heart SCHAD determined in this paper, has demonstrated that the previously published pig heart SCHAD sequence was incorrect. Presented here are the corrected amino acid sequence and the high resolution crystal structure determined for pig heart SCHAD complexed with its NAD+ cofactor (2.8 A; R(cryst) = 22.4%, R(free) = 28.8%). In addition, the peculiar phenomenon of a dimeric enzyme crystallizing with three subunits contained in the asymmetric unit is described.