1h18
From Proteopedia
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PYRUVATE FORMATE-LYASE (E.COLI) IN COMPLEX WITH PYRUVATE
Overview
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.
About this Structure
1H18 is a Single protein structure of sequence from Escherichia coli with , , and as ligands. Active as Formate C-acetyltransferase, with EC number 2.3.1.54 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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., Becker A, Kabsch W, J Biol Chem. 2002 Oct 18;277(42):40036-42. Epub 2002 Aug 5. PMID:12163496
Page seeded by OCA on Sun Feb 3 09:45:03 2008
Categories: Escherichia coli | Formate C-acetyltransferase | Single protein | Becker, A. | Kabsch, W. | DTL | NA | PG4 | PYR | Acetylation | Acyltransferase | Glycyl radical enzyme | Lyase | Transferase
