1mzo: Difference between revisions

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[[Image:1mzo.~~jpg~~|left|200px]]

[[Image:1mzo.png|left|200px]]

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~~'''~~Crystal structure of pyruvate formate-lyase with pyruvate~~'''~~

===Crystal structure of pyruvate formate-lyase with pyruvate===

~~==Overview==~~

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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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_12454503}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12454503 is the PubMed ID number.

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==About this Structure==

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[[Category: Leppanen, V M.]]

[[Category: Enzyme-substrate complex]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3~~ 01:54:32 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:34:28 2008''

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-[[Image:1mzo.jpg|left|200px]]
+{{Seed}}
+[[Image:1mzo.png|left|200px]]
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 {{STRUCTURE_1mzo|  PDB=1mzo  |  SCENE=  }}
-'''Crystal structure of pyruvate formate-lyase with pyruvate'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12454503}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12454503 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12454503}}
 ==About this Structure==
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 [[Category: Leppanen, V M.]]
 [[Category: Enzyme-substrate complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:54:32 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:34:28 2008''