1w88

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Image:1w88.gif


PDB ID 1w88

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, resolution 2.30Å
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

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