1w88
From Proteopedia
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|PDB= 1w88 |SIZE=350|CAPTION= <scene name='initialview01'>1w88</scene>, resolution 2.30Å | |PDB= 1w88 |SIZE=350|CAPTION= <scene name='initialview01'>1w88</scene>, resolution 2.30Å | ||
|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+G'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+G'>AC1</scene> | ||
- | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1w88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w88 OCA], [http://www.ebi.ac.uk/pdbsum/1w88 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w88 RCSB]</span> | ||
}} | }} | ||
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[[Category: Perham, R N.]] | [[Category: Perham, R N.]] | ||
[[Category: Pratap, J V.]] | [[Category: Pratap, J V.]] | ||
- | [[Category: | + | [[Category: catalysis,slinky]] |
- | + | [[Category: dihydrolipoyl,acetyl transferase]] | |
- | [[Category: acetyl transferase | + | |
- | + | ||
- | + | ||
[[Category: multienzyme complex]] | [[Category: multienzyme complex]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
[[Category: pyruvate dehydrogenase]] | [[Category: pyruvate dehydrogenase]] | ||
- | [[Category: slinky]] | ||
[[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 00:32:34 2008'' |
Revision as of 21:32, 30 March 2008
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, resolution 2.30Å | |||||||
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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(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. 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 00:32:34 2008
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. | Catalysis,slinky | Dihydrolipoyl,acetyl transferase | Multienzyme complex | Oxidoreductase | Pyruvate dehydrogenase | Transferase