1w88

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[[Image:1w88.gif|left|200px]]<br />
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[[Image:1w88.gif|left|200px]]<br /><applet load="1w88" size="450" color="white" frame="true" align="right" spinBox="true"
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<applet load="1w88" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1w88, resolution 2.30&Aring;" />
caption="1w88, resolution 2.30&Aring;" />
'''THE CRYSTAL STRUCTURE OF PYRUVATE DEHYDROGENASE E1(D180N, E183Q) BOUND TO THE PERIPHERAL SUBUNIT BINDING DOMAIN OF E2'''<br />
'''THE CRYSTAL STRUCTURE OF PYRUVATE DEHYDROGENASE E1(D180N, E183Q) BOUND TO THE PERIPHERAL SUBUNIT BINDING DOMAIN OF E2'''<br />
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==About this Structure==
==About this Structure==
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1W88 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 and TDP 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=1W88 OCA].
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1W88 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 and TDP 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] Known structural/functional Site: <scene name='pdbsite=AC1:Mg Binding Site For Chain G'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W88 OCA].
==Reference==
==Reference==
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 17:28:45 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:34:03 2007''

Revision as of 16:24, 18 December 2007


1w88, resolution 2.30Å

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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.

About this Structure

1W88 is a Protein complex structure of sequences from Geobacillus stearothermophilus with MG and TDP as ligands. Active as Pyruvate dehydrogenase (acetyl-transferring), with EC number 1.2.4.1 Known structural/functional Site: . 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

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