1mzo
From Proteopedia
(New page: 200px<br /><applet load="1mzo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mzo, resolution 2.7Å" /> '''Crystal structure of ...) |
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| - | [[Image:1mzo.jpg|left|200px]]<br /><applet load="1mzo" size=" | + | [[Image:1mzo.jpg|left|200px]]<br /><applet load="1mzo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mzo, resolution 2.7Å" /> | caption="1mzo, resolution 2.7Å" /> | ||
'''Crystal structure of pyruvate formate-lyase with pyruvate'''<br /> | '''Crystal structure of pyruvate formate-lyase with pyruvate'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of inactive pyruvate formate-lyase in complex with a natural | + | 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== | ==About this Structure== | ||
| - | 1MZO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PGE and PYR as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1MZO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PGE:'>PGE</scene> and <scene name='pdbligand=PYR:'>PYR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MZO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Goldman, A.]] | [[Category: Goldman, A.]] | ||
| - | [[Category: Kozarich, J | + | [[Category: Kozarich, J W.]] |
[[Category: Lehtio, L.]] | [[Category: Lehtio, L.]] | ||
| - | [[Category: Leppanen, V | + | [[Category: Leppanen, V M.]] |
[[Category: PGE]] | [[Category: PGE]] | ||
[[Category: PYR]] | [[Category: PYR]] | ||
[[Category: enzyme-substrate complex]] | [[Category: enzyme-substrate complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:00:44 2008'' |
Revision as of 12:00, 21 February 2008
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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 with and as ligands. Active as Formate C-acetyltransferase, with EC number 2.3.1.54 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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