2pfl: Difference between revisions

Revision as of 20:42, 27 July 2008

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File:2pfl.png

Template:STRUCTURE 2pfl

CRYSTAL STRUCTURE OF PFL FROM E.COLICRYSTAL STRUCTURE OF PFL FROM E.COLI

Template:ABSTRACT PUBMED 10504733

About this StructureAbout this Structure

2PFL is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structure and mechanism of the glycyl radical enzyme pyruvate formate-lyase., Becker A, Fritz-Wolf K, Kabsch W, Knappe J, Schultz S, Volker Wagner AF, Nat Struct Biol. 1999 Oct;6(10):969-75. PMID:10504733

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OCA

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-[[Image:2pfl.jpg|left|200px]]
+{{Seed}}
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 {{STRUCTURE_2pfl|  PDB=2pfl  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF PFL FROM E.COLI'''
+===CRYSTAL STRUCTURE OF PFL FROM E.COLI===
-==Overview==
+<!--
-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.
+-->
+{{ABSTRACT_PUBMED_10504733}}
 ==About this Structure==
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 [[Category: Glycyl radical enzyme]]
 [[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 13:00:56 2008''
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