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1w85

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[[Image:1w85.gif|left|200px]]
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{{Seed}}
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[[Image:1w85.png|left|200px]]
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{{STRUCTURE_1w85| PDB=1w85 | SCENE= }}
{{STRUCTURE_1w85| PDB=1w85 | SCENE= }}
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'''THE CRYSTAL STRUCTURE OF PYRUVATE DEHYDROGENASE E1 BOUND TO THE PERIPHERAL SUBUNIT BINDING DOMAIN OF E2'''
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===THE CRYSTAL STRUCTURE OF PYRUVATE DEHYDROGENASE E1 BOUND TO THE PERIPHERAL SUBUNIT BINDING DOMAIN OF E2===
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==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.
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The line below this paragraph, {{ABSTRACT_PUBMED_15514159}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15514159 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15514159}}
==About this Structure==
==About this Structure==
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[[Category: Pyruvate]]
[[Category: Pyruvate]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:17:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:42:23 2008''

Revision as of 09:42, 29 July 2008

Image:1w85.png

Template:STRUCTURE 1w85

THE CRYSTAL STRUCTURE OF PYRUVATE DEHYDROGENASE E1 BOUND TO THE PERIPHERAL SUBUNIT BINDING DOMAIN OF E2

Template:ABSTRACT PUBMED 15514159

About this Structure

1W85 is a Protein complex structure of sequences from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

Reference

A molecular switch and proton wire synchronize the active sites in thiamine enzymes., Frank RA, Titman CM, Pratap JV, Luisi BF, Perham RN, Science. 2004 Oct 29;306(5697):872-6. PMID:15514159

Page seeded by OCA on Tue Jul 29 12:42:23 2008

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