1w88: Difference between revisions

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[[Image:1w88.~~gif~~|left|200px]]

[[Image:1w88.png|left|200px]]

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~~'''~~THE CRYSTAL STRUCTURE OF PYRUVATE DEHYDROGENASE E1(D180N, E183Q) BOUND TO THE PERIPHERAL SUBUNIT BINDING DOMAIN OF E2~~'''~~

===THE CRYSTAL STRUCTURE OF PYRUVATE DEHYDROGENASE E1(D180N, E183Q) BOUND TO THE PERIPHERAL SUBUNIT BINDING DOMAIN OF E2===

~~==Overview==~~

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~~Thiamine diphosphate (ThDP) is used as a cofactor in many key metabolic enzymes. We present evidence that~~ the ~~ThDPs in~~ the ~~two active sites of the E1~~ (~~EC 1.2~~.4.1) ~~component of~~ the ~~pyruvate dehydrogenase complex communicate over a distance of 20 angstroms by reversibly shuttling a proton through an acidic tunnel in the protein~~. ~~This "proton wire" permits the co~~-~~factors to serve reciprocally as general acid/base in catalysis and to switch the conformation of crucial active~~-site peptide loops. This synchronizes the progression of chemical events and can account for the oligomeric organization, conformational asymmetry, and "ping-pong" kinetic properties of E1 and other thiamine-dependent enzymes.

The line below this paragraph, {{ABSTRACT_PUBMED_15514159}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15514159 is the PubMed ID number.

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==About this Structure==

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[[Category: Pyruvate dehydrogenase]]

[[Category: Transferase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 13~~:17:35 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:38:15 2008''

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-[[Image:1w88.gif|left|200px]]
+{{Seed}}
+[[Image:1w88.png|left|200px]]
 <!--
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 {{STRUCTURE_1w88|  PDB=1w88  |  SCENE=  }}
-'''THE CRYSTAL STRUCTURE OF PYRUVATE DEHYDROGENASE E1(D180N, E183Q) BOUND TO THE PERIPHERAL SUBUNIT BINDING DOMAIN OF E2'''
+===THE CRYSTAL STRUCTURE OF PYRUVATE DEHYDROGENASE E1(D180N, E183Q) BOUND TO THE PERIPHERAL SUBUNIT BINDING DOMAIN OF E2===
-==Overview==
+<!--
-Thiamine diphosphate (ThDP) is used as a cofactor in many key metabolic enzymes. We present evidence that the ThDPs in the two active sites of the E1 (EC 1.2.4.1) component of the pyruvate dehydrogenase complex communicate over a distance of 20 angstroms by reversibly shuttling a proton through an acidic tunnel in the protein. This "proton wire" permits the co-factors to serve reciprocally as general acid/base in catalysis and to switch the conformation of crucial active-site peptide loops. This synchronizes the progression of chemical events and can account for the oligomeric organization, conformational asymmetry, and "ping-pong" kinetic properties of E1 and other thiamine-dependent enzymes.
+The line below this paragraph, {{ABSTRACT_PUBMED_15514159}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15514159 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15514159}}
 ==About this Structure==
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 [[Category: Pyruvate dehydrogenase]]
 [[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 13:17:35 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:38:15 2008''