1pda

From Proteopedia

Revision as of 21:35, 20 November 2007

STRUCTURE OF PORPHOBILINOGEN DEAMINASE REVEALS A FLEXIBLE MULTIDOMAIN POLYMERASE WITH A SINGLE CATALYTIC SITE

Overview

The three-domain structure of porphobilinogen deaminase, a key enzyme in, the biosynthetic pathway of tetrapyrroles, has been defined by X-ray, analysis at 1.9 A resolution. Two of the domains structurally resemble the, transferrins and periplasmic binding proteins. The dipyrromethane cofactor, is covalently linked to domain 3 but is bound by extensive salt-bridges, and hydrogen-bonds within the cleft between domains 1 and 2, at a position, corresponding to the binding sites for small-molecule ligands in the, analogous proteins. The X-ray structure and results from site-directed, mutagenesis provide evidence for a single catalytic site. Interdomain, flexibility may aid elongation of the polypyrrole product in the, active-site cleft of the enzyme.

About this Structure

1PDA is a Single protein structure of sequence from Escherichia coli with DPM and ACY as ligands. Active as Hydroxymethylbilane synthase, with EC number 2.5.1.61 Full crystallographic information is available from OCA.

Reference

Structure of porphobilinogen deaminase reveals a flexible multidomain polymerase with a single catalytic site., Louie GV, Brownlie PD, Lambert R, Cooper JB, Blundell TL, Wood SP, Warren MJ, Woodcock SC, Jordan PM, Nature. 1992 Sep 3;359(6390):33-9. PMID:1522882

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