1mzo

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[[Image:1mzo.jpg|left|200px]]
[[Image:1mzo.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1mzo |SIZE=350|CAPTION= <scene name='initialview01'>1mzo</scene>, resolution 2.7&Aring;
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The line below this paragraph, containing "STRUCTURE_1mzo", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1mzo| PDB=1mzo | SCENE= }}
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|RELATEDENTRY=
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|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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}}
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'''Crystal structure of pyruvate formate-lyase with pyruvate'''
'''Crystal structure of pyruvate formate-lyase with pyruvate'''
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[[Category: Lehtio, L.]]
[[Category: Lehtio, L.]]
[[Category: Leppanen, V M.]]
[[Category: Leppanen, V M.]]
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[[Category: enzyme-substrate complex]]
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[[Category: Enzyme-substrate complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:54:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:23:24 2008''
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Revision as of 22:54, 2 May 2008

Image:1mzo.jpg

Template:STRUCTURE 1mzo

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 Page seeded by OCA on Sat May 3 01:54:32 2008

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