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TitleChanges in the allosteric site of human liver pyruvate kinase upon activator binding include the breakage of an intersubunit cation-pi bond.
Journal, issue, pagesActa Crystallogr. ,Sect. F, Vol. 75, Page 461-469, Year 2019
Publish dateJan 14, 2019 (structure data deposition date)
AuthorsMcFarlane, J.S. / Ronnebaum, T.A. / Meneely, K.M. / Chilton, A. / Fenton, A.W. / Lamb, A.L.
External linksActa Crystallogr. ,Sect. F / PubMed:31204694
MethodsX-ray diffraction
Resolution2.15 - 2.416 Å
Structure data

PDB-6nn4:
The structure of human liver pyruvate kinase, hLPYK-D499N, in complex with Fru-1,6-BP
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

PDB-6nn5:
The structure of human liver pyruvate kinase, hLPYK-W527H
Method: X-RAY DIFFRACTION / Resolution: 2.256 Å

PDB-6nn7:
The structure of human liver pyruvate kinase, hLPYK-GGG
Method: X-RAY DIFFRACTION / Resolution: 2.32 Å

PDB-6nn8:
The structure of human liver pyruvate kinase, hLPYK-S531E
Method: X-RAY DIFFRACTION / Resolution: 2.416 Å

Chemicals

ChemComp-FBP:
1,6-di-O-phosphono-beta-D-fructofuranose

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-PEP:
PHOSPHOENOLPYRUVATE

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-FLC:
CITRATE ANION

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / pyruvate kinase / allosteric / glycolysis

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