1F17

L-3-HYDROXYACYL-COA DEHYDROGENASE COMPLEXED WITH NADH

Summary for 1F17

• Entry DOI: 10.2210/pdb1f17/pdb
• Related: 1F0Y 1F12 1F14 3HAD
• Descriptor: L-3-HYDROXYACYL-COA DEHYDROGENASE, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: l-3-hydroxyacyl-coa dehydrogenase complexed with nadh, oxidoreductase
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion matrix: Q16836
• Total number of polymer chains: 2
• Total formula weight: 69122.53

Authors

Barycki, J.J.,O'Brien, L.K.,Strauss, A.W.,Banaszak, L.J. (deposition date: 2000-05-18, release date: 2000-09-27, Last modification date: 2024-02-07)

Primary citation

Barycki, J.J.,O'Brien, L.K.,Strauss, A.W.,Banaszak, L.J.
Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase.
J.Biol.Chem., 275:27186-27196, 2000

PubMed Abstract: l-3-Hydroxyacyl-CoA dehydrogenase reversibly catalyzes the conversion of l-3-hydroxyacyl-CoA to 3-ketoacyl-CoA concomitant with the reduction of NAD(+) to NADH as part of the beta-oxidation spiral. In this report, crystal structures have been solved for the apoenzyme, binary complexes of the enzyme with reduced cofactor or 3-hydroxybutyryl-CoA substrate, and an abortive ternary complex of the enzyme with NAD(+) and acetoacetyl-CoA. The models illustrate positioning of cofactor and substrate within the active site of the enzyme. Comparison of these structures with the previous model of the enzyme-NAD(+) complex reveals that although significant shifting of the NAD(+)-binding domain relative to the C-terminal domain occurs in the ternary and substrate-bound complexes, there are few differences between the apoenzyme and cofactor-bound complexes. Analysis of these models clarifies the role of key amino acids implicated in catalysis and highlights additional critical residues. Furthermore, a novel charge transfer complex has been identified in the course of abortive ternary complex formation, and its characterization provides additional insight into aspects of the catalytic mechanism of l-3-hydroxyacyl-CoA dehydrogenase.

PubMed: 10840044

Experimental method

X-RAY DIFFRACTION (2.3 Å)