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Structure paper

TitleA Dimer Interface Mutation in Glyceraldehyde-3-Phosphate Dehydrogenase Regulates Its Binding to AU-rich RNA.
Journal, issue, pagesJ. Biol. Chem., Vol. 290, Page 1770-1785, Year 2015
Publish dateOct 11, 2014 (structure data deposition date)
AuthorsWhite, M.R. / Khan, M.M. / Deredge, D. / Ross, C.R. / Quintyn, R. / Zucconi, B.E. / Wysocki, V.H. / Wintrode, P.L. / Wilson, G.M. / Garcin, E.D.
External linksJ. Biol. Chem. / PubMed:25451934
MethodsX-ray diffraction
Resolution1.99 - 2.3 Å
Structure data

PDB-4wnc:
Crystal structure of human wild-type GAPDH at 1.99 angstroms resolution
Method: X-RAY DIFFRACTION / Resolution: 1.99 Å

PDB-4wni:
Crystal structure of the T229K mutant of human GAPDH at 2.3 angstroems resolution
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-ZN:
Unknown entry

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / glycolytic / Rossman fold / NAD-binding / NAD cofactor / mutant

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