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Structure paper

TitleA Spring Loaded Release Mechanism Regulates Domain Movement and Catalysis in Phosphoglycerate Kinase.
Journal, issue, pagesJ. Biol. Chem., Vol. 286, Page 14040-, Year 2011
Publish dateMay 11, 2010 (structure data deposition date)
AuthorsZerrad, L. / Merli, A. / Schroder, G.F. / Varga, A. / Graczer, E. / Pernot, P. / Round, A. / Vas, M. / Bowler, M.W.
External linksJ. Biol. Chem. / PubMed:21349853
MethodsX-ray diffraction
Resolution1.74 - 2.2 Å
Structure data

PDB-2xe6:
The complete reaction cycle of human phosphoglycerate kinase: The open binary complex with 3PG
Method: X-RAY DIFFRACTION / Resolution: 1.74 Å

PDB-2xe7:
The complete reaction cycle of human phosphoglycerate kinase: The open ternary complex with 3PG and ADP
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-2xe8:
The complete reaction cycle of human phosphoglycerate kinase: The open ternary complex with 3PG and AMP-PNP
Method: X-RAY DIFFRACTION / Resolution: 1.79 Å

Chemicals

ChemComp-3PG:
3-PHOSPHOGLYCERIC ACID

ChemComp-HOH:
WATER

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

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

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / TRANSITION STATE ANALOGUE / HEREDITARY HEMOLYTIC ANEMIA / PHOSPHOPROTEIN / GLYCOLYSIS / PHOSPHORYL TRANSFER / NUCLEOTIDE-BINDING / DOMAIN MOTIONS / KINASE

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