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Structure paper

TitleCrystal structures of Escherichia coli glycerol kinase variant S58-->W in complex with nonhydrolyzable ATP analogues reveal a putative active conformation of the enzyme as a result of domain motion.
Journal, issue, pagesBiochemistry, Vol. 38, Page 3508-3518, Year 1999
Publish dateSep 23, 1998 (structure data deposition date)
AuthorsBystrom, C.E. / Pettigrew, D.W. / Branchaud, B.P. / O'Brien, P. / Remington, S.J.
External linksBiochemistry / PubMed:10090737
MethodsX-ray diffraction
Resolution3 Å
Structure data

PDB-1bwf:
ESCHERICHIA COLI GLYCEROL KINASE MUTANT WITH BOUND ATP ANALOG SHOWING SUBSTANTIAL DOMAIN MOTION
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-1glj:
ESCHERICHIA COLI GLYCEROL KINASE MUTANT WITH BOUND ATP ANALOG SHOWING SUBSTANTIAL DOMAIN MOTION
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-1gll:
ESCHERICHIA COLI GLYCEROL KINASE MUTANT WITH BOUND ATP ANALOG SHOWING SUBSTANTIAL DOMAIN MOTION
Method: X-RAY DIFFRACTION / Resolution: 3 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ATF:
PHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER

ChemComp-GOL:
GLYCEROL

ChemComp-ATS:
GAMMA-ARSONO-BETA, GAMMA-METHYLENEADENOSINE-5'-DIPHOSPHATE

ChemComp-ACP:
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / AMP-PCP, energy-carrying molecule analogue*YM

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / KINASE / DOMAIN MOTION / ALLOSTERIC REGULATION HYDROLASE / LIPID DEGRADATION / PLATELET FACTOR / PHOSPHOTRANSFERASE / ALLOSTERIC REGULATION

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