1mzo
From Proteopedia
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|PDB= 1mzo |SIZE=350|CAPTION= <scene name='initialview01'>1mzo</scene>, resolution 2.7Å | |PDB= 1mzo |SIZE=350|CAPTION= <scene name='initialview01'>1mzo</scene>, resolution 2.7Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene> | + | |LIGAND= <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</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=1mzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mzo OCA], [http://www.ebi.ac.uk/pdbsum/1mzo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mzo RCSB]</span> | ||
}} | }} | ||
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[[Category: Lehtio, L.]] | [[Category: Lehtio, L.]] | ||
[[Category: Leppanen, V M.]] | [[Category: Leppanen, V M.]] | ||
| - | [[Category: PGE]] | ||
| - | [[Category: PYR]] | ||
[[Category: enzyme-substrate complex]] | [[Category: enzyme-substrate complex]] | ||
| - | ''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 22:23:24 2008'' |
Revision as of 19:23, 30 March 2008
| |||||||
| , resolution 2.7Å | |||||||
|---|---|---|---|---|---|---|---|
| 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 pyruvate formate-lyase with pyruvate
Overview
The structure of inactive pyruvate formate-lyase in complex with a natural substrate, pyruvate, was solved at 2.7 A resolution. Both active sites of the homodimeric enzyme are occupied by pyruvate; additional binding sites were not found. Pyruvate was found in a cleft close to the active-site cysteines 418 and 419, with the carboxyl group in contact with arginines 176 and 435 and the methyl group within van der Waals distance of Phe327. It is believed that the binding site of pyruvate is not the position of pyruvate as the reaction initiates, as conformational changes occur during activation of the enzyme.
About this Structure
1MZO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of Escherichia coli pyruvate formate-lyase with pyruvate., Lehtio L, Leppanen VM, Kozarich JW, Goldman A, Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2209-12. Epub 2002, Nov 23. PMID:12454503
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