1w85: Difference between revisions
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[[Image:1w85.gif|left|200px]] | [[Image:1w85.gif|left|200px]] | ||
'''THE CRYSTAL STRUCTURE OF PYRUVATE DEHYDROGENASE E1 BOUND TO THE PERIPHERAL SUBUNIT BINDING DOMAIN OF E2''' | {{Structure | ||
|PDB= 1w85 |SIZE=350|CAPTION= <scene name='initialview01'>1w85</scene>, resolution 2.00Å | |||
|SITE= <scene name='pdbsite=AC1:Tdp+Binding+Site+For+Chain+G'>AC1</scene> | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=TDP:THIAMIN+DIPHOSPHATE'>TDP</scene> and <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''THE CRYSTAL STRUCTURE OF PYRUVATE DEHYDROGENASE E1 BOUND TO THE PERIPHERAL SUBUNIT BINDING DOMAIN OF E2''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1W85 is a [ | 1W85 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.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:// | 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://www.ncbi.nlm.nih.gov/pubmed/15514159 15514159] | ||
[[Category: Geobacillus stearothermophilus]] | [[Category: Geobacillus stearothermophilus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:53:29 2008'' | ||
Revision as of 12:53, 20 March 2008
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| 1w85, resolution 2.00Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | MG, K, TDP and PEG | ||||||||||||
| Activity: | Pyruvate dehydrogenase (acetyl-transferring), with EC number 1.2.4.1 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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