1qs0

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(New page: 200px<br /><applet load="1qs0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qs0, resolution 2.40&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 22:48, 20 November 2007


1qs0, resolution 2.40Å

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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 with MG, COI and TDP as ligands. 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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