1QHM

ESCHERICHIA COLI PYRUVATE FORMATE LYASE LARGE DOMAIN

Summary for 1QHM

• Entry DOI: 10.2210/pdb1qhm/pdb
• Descriptor: PYRUVATE FORMATE-LYASE (2 entities in total)
• Functional Keywords: pyruvate formate lyase, anaerobic, homodimer, enzyme mechanism, lyase-transferase complex, lyase/transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P09373
• Total number of polymer chains: 2
• Total formula weight: 141078.36

Authors

Leppanen, V.-M.,Merckel, M.C.,Ollis, D.L.,Wong, K.K.,Kozarich, J.W.,Goldman, A. (deposition date: 1999-05-19, release date: 2000-05-24, Last modification date: 2023-12-27)

Primary citation

Leppanen, V.M.,Merckel, M.C.,Ollis, D.L.,Wong, K.K.,Kozarich, J.W.,Goldman, A.
Pyruvate formate lyase is structurally homologous to type I ribonucleotide reductase.
Structure Fold.Des., 7:733-744, 1999

PubMed Abstract: Pyruvate formate lyase (PFL) catalyses a key step in Escherichia coli anaerobic glycolysis by converting pyruvate and CoA to formate and acetylCoA. The PFL mechanism involves an unusual radical cleavage of pyruvate, involving an essential C alpha radical of Gly734 and two cysteine residues, Cys418 and Cys419, which may form thiyl radicals required for catalysis. We undertook this study to understand the structural basis for catalysis.

PubMed: 10425676
DOI: 10.1016/S0969-2126(99)80098-7

Experimental method

X-RAY DIFFRACTION (2.8 Å)