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| [[Image:2pfl.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2pfl| PDB=2pfl | SCENE= }} | | {{STRUCTURE_2pfl| PDB=2pfl | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF PFL FROM E.COLI'''
| | ===CRYSTAL STRUCTURE OF PFL FROM E.COLI=== |
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| ==Overview==
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| Pyruvate formate-lyase (PFL) from Escherichia coli uses a radical mechanism to reversibly cleave the C1-C2 bond of pyruvate using the Gly 734 radical and two cysteine residues (Cys 418, Cys 419). We have determined by X-ray crystallography the structures of PFL (non-radical form), its complex with the substrate analog oxamate, and the C418A,C419A double mutant. The atomic model (a dimer of 759-residue monomers) comprises a 10-stranded beta/alpha barrel assembled in an antiparallel manner from two parallel five-stranded beta-sheets; this architecture resembles that of ribonucleotide reductases. Gly 734 and Cys 419, positioned at the tips of opposing hairpin loops, meet in the apolar barrel center (Calpha-Sgamma = 3.7 A). Oxamate fits into a compact pocket where C2 is juxtaposed with Cys 418Sgamma (3.3 A), which in turn is close to Cys 419Sgamma (3.7 A). Our model of the active site is suggestive of a snapshot of the catalytic cycle, when the pyruvate-carbonyl awaits attack by the Cys 418 thiyl radical. We propose a homolytic radical mechanism for PFL that involves Cys 418 and Cys 419 both as thiyl radicals, with distinct chemical functions.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10504733}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10504733 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10504733}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Glycyl radical enzyme]] | | [[Category: Glycyl radical enzyme]] |
| [[Category: Transferase]] | | [[Category: Transferase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:00:56 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:42:37 2008'' |
