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PDBsum entry 3hdh
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Oxidoreductase
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PDB id
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3hdh
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Pig heart short chain l-3-Hydroxyacyl-Coa dehydrogenase revisited: sequence analysis and crystal structure determination.
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Authors
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J.J.Barycki,
L.K.O'Brien,
J.J.Birktoft,
A.W.Strauss,
L.J.Banaszak.
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Ref.
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Protein Sci, 1999,
8,
2010-2018.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Secondary reference #1
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Title
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Structure of l-3-Hydroxyacyl-Coenzyme a dehydrogenase: preliminary chain tracing at 2.8-A resolution.
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Authors
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J.J.Birktoft,
H.M.Holden,
R.Hamlin,
N.H.Xuong,
L.J.Banaszak.
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Ref.
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Proc Natl Acad Sci U S A, 1987,
84,
8262-8266.
[DOI no: ]
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PubMed id
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