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Structure paper

TitlePyruvate Kinase Regulates the Pentose-Phosphate Pathway in Response to Hypoxia in Mycobacterium tuberculosis.
Journal, issue, pagesJ. Mol. Biol., Vol. 431, Page 3690-3705, Year 2019
Publish dateNov 24, 2018 (structure data deposition date)
AuthorsZhong, W. / Guo, J. / Cui, L. / Chionh, Y.H. / Li, K. / El Sahili, A. / Cai, Q. / Yuan, M. / Michels, P.A.M. / Fothergill-Gilmore, L.A. ...Zhong, W. / Guo, J. / Cui, L. / Chionh, Y.H. / Li, K. / El Sahili, A. / Cai, Q. / Yuan, M. / Michels, P.A.M. / Fothergill-Gilmore, L.A. / Walkinshaw, M.D. / Mu, Y. / Lescar, J. / Dedon, P.C.
External linksJ. Mol. Biol. / PubMed:31381898
MethodsX-ray diffraction
Resolution2.55 Å
Structure data

PDB-6ito:
Crystal structure of pyruvate kinase (PYK) from Mycobacterium tuberculosis in complex with Oxalate, AMP and inhibitor Ribose 5-Phosphate
Method: X-RAY DIFFRACTION / Resolution: 2.55 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-OXL:
OXALATE ION

ChemComp-R5P:
RIBOSE-5-PHOSPHATE

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-HOH:
WATER

Source
  • mycobacterium tuberculosis (strain atcc 25618 / h37rv) (bacteria)
KeywordsTRANSFERASE / pyruvate kinase / glycolysis / tetramer / allostery / synergism / phospho transferase

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