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1w85

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Image:1w85.gif

1w85, resolution 2.00Å

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THE CRYSTAL STRUCTURE OF PYRUVATE DEHYDROGENASE E1 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

1W85 is a [Protein complex] structure of sequences from [Geobacillus stearothermophilus] with MG, K, TDP and PEG as [ligands]. Active as [Pyruvate dehydrogenase (acetyl-transferring)], with EC number [1.2.4.1]. Structure known Active Site: AC1. 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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