2ii3: Difference between revisions
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|PDB= 2ii3 |SIZE=350|CAPTION= <scene name='initialview01'>2ii3</scene>, resolution 2.170Å | |PDB= 2ii3 |SIZE=350|CAPTION= <scene name='initialview01'>2ii3</scene>, resolution 2.170Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CAO:OXIDIZED+COENZYME+A'>CAO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_(2-methylpropanoyl)transferase Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.168 2.3.1.168] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_(2-methylpropanoyl)transferase Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.168 2.3.1.168] </span> | ||
|GENE= DBT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | |GENE= DBT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2ihw|2IHW]], [[2ii4|2II4]], [[2ii5|2II5]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ii3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ii3 OCA], [http://www.ebi.ac.uk/pdbsum/2ii3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ii3 RCSB]</span> | |||
}} | }} | ||
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[[Category: Kato, M.]] | [[Category: Kato, M.]] | ||
[[Category: Wynn, R M.]] | [[Category: Wynn, R M.]] | ||
[[Category: cubic core]] | [[Category: cubic core]] | ||
[[Category: homo trimer]] | [[Category: homo trimer]] | ||
[[Category: oxidized coa-bound form]] | [[Category: oxidized coa-bound form]] | ||
''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 03:44:42 2008'' | ||
Revision as of 03:44, 31 March 2008
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| , resolution 2.170Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | DBT (Bos taurus) | ||||||
| Activity: | Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase, with EC number 2.3.1.168 | ||||||
| Related: | 2IHW, 2II4, 2II5
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of a cubic core of the dihydrolipoamide acyltransferase (E2b) component in the branched-chain alpha-ketoacid dehydrogenase complex (BCKDC), Oxidized Coenzyme A-bound form
OverviewOverview
The dihydrolipoamide acyltransferase (E2b) component of the branched-chain alpha-ketoacid dehydrogenase complex forms a cubic scaffold that catalyzes acyltransfer from S-acyldihydrolipoamide to CoA to produce acyl-CoA. We have determined the first crystal structures of a mammalian (bovine) E2b core domain with and without a bound CoA or acyl-CoA. These structures reveal both hydrophobic and the previously unreported ionic interactions between two-fold-related trimers that build up the cubic core. The entrance of the dihydrolipoamide-binding site in a 30-A long active-site channel is closed in the apo and acyl-CoA-bound structures. CoA binding to one entrance of the channel promotes a conformational change in the channel, resulting in the opening of the opposite dihydrolipoamide gate. Binding experiments show that the affinity of the E2b core for dihydrolipoamide is markedly increased in the presence of CoA. The result buttresses the model that CoA binding is responsible for the opening of the dihydrolipoamide gate. We suggest that this gating mechanism synchronizes the binding of the two substrates to the active-site channel, which serves as a feed-forward switch to coordinate the E2b-catalyzed acyltransfer reaction.
About this StructureAbout this Structure
2II3 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
A synchronized substrate-gating mechanism revealed by cubic-core structure of the bovine branched-chain alpha-ketoacid dehydrogenase complex., Kato M, Wynn RM, Chuang JL, Brautigam CA, Custorio M, Chuang DT, EMBO J. 2006 Dec 13;25(24):5983-94. Epub 2006 Nov 23. PMID:17124494
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