1cm5
From Proteopedia
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|PDB= 1cm5 |SIZE=350|CAPTION= <scene name='initialview01'>1cm5</scene>, resolution 2.3Å | |PDB= 1cm5 |SIZE=350|CAPTION= <scene name='initialview01'>1cm5</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene> | + | |LIGAND= <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cm5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cm5 OCA], [http://www.ebi.ac.uk/pdbsum/1cm5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cm5 RCSB]</span> | ||
}} | }} | ||
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[[Category: Schultz, S.]] | [[Category: Schultz, S.]] | ||
[[Category: Wagner, A F.V.]] | [[Category: Wagner, A F.V.]] | ||
| - | [[Category: CO3]] | ||
| - | [[Category: NA]] | ||
[[Category: glucose metabolism]] | [[Category: glucose metabolism]] | ||
[[Category: glycyl radical enzyme]] | [[Category: glycyl radical enzyme]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:24:26 2008'' |
Revision as of 16:24, 30 March 2008
| |||||||
| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Formate C-acetyltransferase, with EC number 2.3.1.54 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF C418A,C419A MUTANT 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.
About this Structure
1CM5 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
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:10504733
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