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1w85
From Proteopedia
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|PDB= 1w85 |SIZE=350|CAPTION= <scene name='initialview01'>1w85</scene>, resolution 2.00Å | |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> | |SITE= <scene name='pdbsite=AC1:Tdp+Binding+Site+For+Chain+G'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=TDP:THIAMIN+DIPHOSPHATE'>TDP</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w85 OCA], [http://www.ebi.ac.uk/pdbsum/1w85 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w85 RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Perham, R N.]] | [[Category: Perham, R N.]] | ||
[[Category: Pratap, J V.]] | [[Category: Pratap, J V.]] | ||
| - | [[Category: K]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: PEG]] | ||
| - | [[Category: TDP]] | ||
[[Category: acetyl transferase]] | [[Category: acetyl transferase]] | ||
[[Category: dehydrogenase]] | [[Category: dehydrogenase]] | ||
| Line 40: | Line 39: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:32:32 2008'' |
Revision as of 21:32, 30 March 2008
| |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , | ||||||
| Activity: | Pyruvate dehydrogenase (acetyl-transferring), with EC number 1.2.4.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Mon Mar 31 00:32:32 2008
