D-Glyceraldehyde-3-Phosphate Dehydrogenase: Three-Dimensional Structure and Evolutionary Significance

A 3.0- angstrom resolution electron density map of lobster glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) was computed. The essentially single isomorphous replacement map was very substantially improved by averaging subunits. NAD binds in an open conformation at sites close to subunit interf...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1973-11, Vol.70 (11), p.3052-3054
Main Authors: Buehner, Manfred, Ford, Geoffrey C., Moras, Dino, Olsen, Kenneth W., Rossmann, Michael G.
Format: Article
Language:English
Subjects:
Alcohols
Animals
Binding Sites
Biological Evolution
Biological Sciences: Biochemistry
Coenzymes
Dehydrogenases
Dimers
Electron density
Enzymes
Evolution
Genetic Code
Glyceraldehyde-3-Phosphate Dehydrogenases
L-Lactate Dehydrogenase
Lactates
Liver
Models, Structural
NAD
Nephropidae
Protein Conformation
Proteins
X-Ray Diffraction
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Summary:A 3.0- angstrom resolution electron density map of lobster glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) was computed. The essentially single isomorphous replacement map was very substantially improved by averaging subunits. NAD binds in an open conformation at sites close to subunit interfaces. The coenzyme binding portion of the enzyme has almost the same fold as the corresponding portion of lactate dehydrogenase (EC 1.1.1.27). The presence of this structure in the five enzymes, analyzed so far, that use nucleotide coenzymes might indicate a fundamental primordial structural element.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.70.11.3052