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PMID: 6930651 Published · ppublish English Journal Article

Three-dimensional structure of a pyridoxal-phosphate-dependent enzyme, mitochondrial aspartate aminotransferase.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 77 ·No. 5 ·1980-05-00 ·Pages 2559-63

Ford GC, Eichele G, Jansonius JN

Abstract

X-ray diffraction studies to 2.8-A resolution have yielded the three-dimensional structure of mitochondrial aspartate aminotransferase (L-aspartate:2-oxoglutarate aminotransferase, EC 2.6.1.1), an isologous alpha 2 dimer (Mr = 2 x 45,000). The subunits are rich in secondary structure and contain two domains, one of which anchors the coenzyme, pyridoxal 5'-phosphate. Each active site lies between the subunits and is composed of residues from both of them.

MeSH Terms
Animals Aspartate Aminotransferases/metabolism Binding Sites Chickens Hydrogen Bonding Macromolecular Substances Mitochondria/enzymology Models, Molecular Protein Conformation Pyridoxal Phosphate/metabolism X-Ray Diffraction
Chemicals
Macromolecular Substances Pyridoxal Phosphate Aspartate Aminotransferases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Ford G C
Eichele G
Jansonius J N
References (46)
46 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.77.5.2559
Published
1980-05-00
Pages
2559-63
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC349441
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.77.5.2559 PMC Full Text View journal details
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