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TitleEvolutionary plasticity in the allosteric regulator-binding site of pyruvate kinase isoform PykA fromPseudomonas aeruginosa.
Journal, issue, pagesJ. Biol. Chem., Vol. 294, Page 15505-15516, Year 2019
Publish dateMar 7, 2019 (structure data deposition date)
AuthorsAbdelhamid, Y. / Brear, P. / Greenhalgh, J. / Chee, X. / Rahman, T. / Welch, M.
External linksJ. Biol. Chem. / PubMed:31484721
MethodsX-ray diffraction
Resolution2.43 Å
Structure data

PDB-6qxl:
Crystal Structure of Pyruvate Kinase II (PykA) from Pseudomonas aeruginosa in complex with sodium malonate, magnesium and glucose-6-phosphate
Method: X-RAY DIFFRACTION / Resolution: 2.43 Å

Chemicals

ChemComp-G6P:
6-O-phosphono-alpha-D-glucopyranose

ChemComp-MG:
Unknown entry

ChemComp-MLI:
MALONATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • pseudomonas aeruginosa (bacteria)
KeywordsTRANSFERASE / Pyruvate kinase / PykA / homotetramer / polypeptide / G6P-bound / PykA-MLI-Mg complex

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