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TitleGlycerol kinase from Escherichia coli and an Ala65-->Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation.
Journal, issue, pagesStructure, Vol. 6, Page 1407-1418, Year 1998
Publish dateAug 30, 1998 (structure data deposition date)
AuthorsFeese, M.D. / Faber, H.R. / Bystrom, C.E. / Pettigrew, D.W. / Remington, S.J.
External linksStructure / PubMed:9817843
MethodsX-ray diffraction
Resolution2.37 - 2.62 Å
Structure data

PDB-1bu6:
CRYSTAL STRUCTURES OF ESCHERICHIA COLI GLYCEROL KINASE AND THE MUTANT A65T IN AN INACTIVE TETRAMER: CONFORMATIONAL CHANGES AND IMPLICATIONS FOR ALLOSTERIC REGULATION
Method: X-RAY DIFFRACTION / Resolution: 2.37 Å

PDB-1glf:
CRYSTAL STRUCTURES OF ESCHERICHIA COLI GLYCEROL KINASE AND THE MUTANT A65T IN AN INACTIVE TETRAMER: CONFORMATIONAL CHANGES AND IMPLICATIONS FOR ALLOSTERIC REGULATION
Method: X-RAY DIFFRACTION / Resolution: 2.62 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / ALLOSTERY / COOPERATIVITY / GLYCEROL KINASE

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