1qs0
From Proteopedia
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|PDB= 1qs0 |SIZE=350|CAPTION= <scene name='initialview01'>1qs0</scene>, resolution 2.40Å | |PDB= 1qs0 |SIZE=350|CAPTION= <scene name='initialview01'>1qs0</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=COI:2-OXO-4-METHYLPENTANOIC+ACID'>COI</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=TDP:THIAMIN+DIPHOSPHATE'>TDP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qs0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qs0 OCA], [http://www.ebi.ac.uk/pdbsum/1qs0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qs0 RCSB]</span> | ||
}} | }} | ||
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[[Category: Sokatch, J R.]] | [[Category: Sokatch, J R.]] | ||
[[Category: Turley, S.]] | [[Category: Turley, S.]] | ||
| - | [[Category: COI]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: TDP]] | ||
[[Category: heterotetramer]] | [[Category: heterotetramer]] | ||
[[Category: thdp cofactor]] | [[Category: thdp cofactor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:18:10 2008'' |
Revision as of 20:18, 30 March 2008
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| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF PSEUDOMONAS PUTIDA 2-OXOISOVALERATE DEHYDROGENASE (BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE, E1B)
Overview
The family of giant multienzyme complexes metabolizing pyruvate, 2-oxoglutarate, branched-chain 2-oxo acids or acetoin contains several of the largest and most sophisticated protein assemblies known, with molecular masses between 4 and 10 million Da. The principal enzyme components, E1, E2 and E3, are present in numerous copies and utilize multiple cofactors to catalyze a directed sequence of reactions via substrate channeling. The crystal structure of a heterotetrameric (alpha2beta2) E1, 2-oxoisovalerate dehydrogenase from Pseudomonas putida, reveals a tightly packed arrangement of the four subunits with the beta2-dimer held between the jaws of a 'vise' formed by the alpha2-dimer. A long hydrophobic channel, suitable to accommodate the E2 lipoyl-lysine arm, leads to the active site, which contains the cofactor thiamin diphosphate (ThDP) and an inhibitor-derived covalent modification of a histidine side chain. The E1 structure, together with previous structural information on E2 and E3, completes the picture of the shared architectural features of these enormous macromolecular assemblies.
About this Structure
1QS0 is a Protein complex structure of sequences from Pseudomonas putida. Full crystallographic information is available from OCA.
Reference
Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes., Aevarsson A, Seger K, Turley S, Sokatch JR, Hol WG, Nat Struct Biol. 1999 Aug;6(8):785-92. PMID:10426958
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