1cm5: Difference between revisions
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'''CRYSTAL STRUCTURE OF C418A,C419A MUTANT OF PFL FROM E.COLI''' | {{Structure | ||
|PDB= 1cm5 |SIZE=350|CAPTION= <scene name='initialview01'>1cm5</scene>, resolution 2.3Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene> and <scene name='pdbligand=NA:SODIUM ION'>NA</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Formate_C-acetyltransferase Formate C-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.54 2.3.1.54] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF C418A,C419A MUTANT OF PFL FROM E.COLI''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CM5 is a [ | 1CM5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CM5 OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10504733 10504733] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Formate C-acetyltransferase]] | [[Category: Formate C-acetyltransferase]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:26:06 2008'' | ||
Revision as of 11:26, 20 March 2008
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| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Formate C-acetyltransferase, with EC number 2.3.1.54 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF C418A,C419A MUTANT OF PFL FROM E.COLI
OverviewOverview
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.
About this StructureAbout this Structure
1CM5 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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