1H18

Pyruvate Formate-Lyase (E.coli) in complex with Pyruvate

Summary for 1H18

• Entry DOI: 10.2210/pdb1h18/pdb
• Related: 1CM5 1H16 1H17 1QHM 2PFL 3PFL
• Descriptor: FORMATE ACETYLTRANSFERASE 1, PYRUVIC ACID, SODIUM ION, ... (6 entities in total)
• Functional Keywords: lyase, glycyl radical enzyme, transferase, acyltransferase, acetylation
• Biological source: ESCHERICHIA COLI
• Cellular location: Cytoplasm: P09373
• Total number of polymer chains: 2
• Total formula weight: 172452.46

Authors

Becker, A.,Kabsch, W. (deposition date: 2002-07-04, release date: 2002-11-01, Last modification date: 2023-12-13)

Primary citation

Becker, A.,Kabsch, W.
X-Ray Structure of Pyruvate Formate-Lyase in Complex with Pyruvate and Coa.How the Enzyme Uses the Cys-418 Thiyl Radical for Pyruvate Cleavage
J.Biol.Chem., 277:40036-, 2002

PubMed Abstract: The glycyl radical enzyme pyruvate formate-lyase (PFL) synthesizes acetyl-CoA and formate from pyruvate and CoA. With the crystal structure of the non-radical form of PFL in complex with its two substrates, we have trapped the moment prior to pyruvate cleavage. The structure reveals how the active site aligns the scissile bond of pyruvate for radical attack, prevents non-radical side reactions of the pyruvate, and confines radical migration. The structure shows CoA in a syn conformation awaiting pyruvate cleavage. By changing to an anti conformation, without affecting the adenine binding mode of CoA, the thiol of CoA could pick up the acetyl group resulting from pyruvate cleavage.

PubMed: 12163496
DOI: 10.1074/JBC.M205821200

Experimental method

X-RAY DIFFRACTION (2.3 Å)