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Structure paper

TitleIsoform-specific regulation of PKM by acetylation
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Year 2025
Publish dateNov 25, 2024 (structure data deposition date)
AuthorsPavlenko, D. / Tamargo-Azpilicueta, J. / Ankri, Y. / Nudelman, H. / Shahar, A. / Diez-Moreno, I. / Arbely, E.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution2.02 - 2.9 Å
Structure data

PDB-9hia:
K115 acetylated human muscle pyruvate kinase, isoform M2 (PKM2), in complex with FBP
Method: X-RAY DIFFRACTION / Resolution: 2.02 Å

PDB-9hib:
K115 acetylated human muscle pyruvate kinase, isoform M2 (PKM2)
Method: X-RAY DIFFRACTION / Resolution: 2.17 Å

PDB-9hic:
K166 acetylated human muscle pyruvate kinase, isoform M2 (PKM2), in complex with FBP
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

Chemicals

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

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-SIN:
SUCCINIC ACID

ChemComp-GOL:
GLYCEROL

ChemComp-K:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / acetylation / post-translational modification / glycolysis / genetic code expansion / acetylated lysine / metabolism

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