1w1z

From Proteopedia

Revision as of 10:51, 30 October 2007

STRUCTURE OF THE PLANT LIKE 5-AMINO LAEVULINIC ACID DEHYDRATASE FROM CHLOROBIUM VIBRIOFORME

Overview

5-Aminolaevulinic acid dehydratase (ALAD), an early enzyme of the, tetrapyrrole biosynthesis pathway, catalyses the dimerisation of, 5-aminolaevulinic acid to form the pyrrole, porphobilinogen. ALAD from, Chlorobium vibrioforme is shown to form a homo-octameric structure with, 422 symmetry in which each subunit adopts a TIM-barrel fold with a 30, residue N-terminal arm extension. Pairs of monomers associate with their, arms wrapped around each other. Four of these dimers interact principally, via their arm regions to form octamers in which each active site is, located on the surface. The active site contains two invariant lysine, residues (200 and 253), one of which (Lys253) forms a Schiff base link, with the bound substrate analogue, laevulinic acid. The carboxyl group of, the laevulinic ... [(full description)]

About this Structure

1W1Z is a [Single protein] structure of sequence from [Prosthecochloris vibrioformis] with MG and LEA as [ligands]. Active as [Porphobilinogen synthase], with EC number [4.2.1.24]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

The X-ray structure of the plant like 5-aminolaevulinic acid dehydratase from Chlorobium vibrioforme complexed with the inhibitor laevulinic acid at 2.6 A resolution., Coates L, Beaven G, Erskine PT, Beale SI, Avissar YJ, Gill R, Mohammed F, Wood SP, Shoolingin-Jordan P, Cooper JB, J Mol Biol. 2004 Sep 10;342(2):563-70. PMID:15327955

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