1w85
From Proteopedia
(New page: 200px<br /> <applet load="1w85" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w85, resolution 2.00Å" /> '''THE CRYSTAL STRUCTU...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1W85 is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/ | + | 1W85 is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]] with MG, K, TDP and PEG as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Pyruvate_dehydrogenase_(acetyl-transferring) Pyruvate dehydrogenase (acetyl-transferring)]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.1 1.2.4.1]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W85 OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15514159 15514159] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15514159 15514159] | ||
| - | [[Category: | + | [[Category: Geobacillus stearothermophilus]] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| + | [[Category: Pyruvate dehydrogenase (acetyl-transferring)]] | ||
[[Category: Frank, R.A.W.]] | [[Category: Frank, R.A.W.]] | ||
[[Category: Luisi, B.F.]] | [[Category: Luisi, B.F.]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:58:53 2007'' |
Revision as of 11:54, 30 October 2007
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THE CRYSTAL STRUCTURE OF PYRUVATE DEHYDROGENASE E1 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.
About this Structure
1W85 is a [Protein complex] structure of sequences from [Geobacillus stearothermophilus] with MG, K, TDP and PEG as [ligands]. Active as [Pyruvate dehydrogenase (acetyl-transferring)], with EC number [1.2.4.1]. Structure known Active Site: AC1. 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 Oct 30 13:58:53 2007
Categories: Geobacillus stearothermophilus | Protein complex | Pyruvate dehydrogenase (acetyl-transferring) | Frank, R.A.W. | Luisi, B.F. | Pei, X.Y. | Perham, R.N. | Pratap, J.V. | K | MG | PEG | TDP | Acetyl transferase | Dehydrogenase | Dihydrolipoyl | Multienzyme complex | Oxidoreductase | Pyruvate | Transferase
