1H17
Pyruvate Formate-Lyase (E.coli) in complex with CoA and the substrate analog oxamate
Summary for 1H17
| Entry DOI | 10.2210/pdb1h17/pdb |
| Related | 1CM5 1H16 1H18 1QHM 2PFL 3PFL |
| Descriptor | FORMATE ACETYLTRANSFERASE 1, COENZYME A, OXAMIC ACID, ... (8 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 | 1 |
| Total formula weight | 87196.63 |
| Authors | Becker, A.,Kabsch, W. (deposition date: 2002-07-03, 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 Cited by 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: 12163496DOI: 10.1074/JBC.M205821200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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