1aw8

From Proteopedia

Revision as of 12:47, 30 October 2007

PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE

Overview

The structure of L-aspartate-alpha-decarboxylase from E. coli has been, determined at 2.2 A resolution. The enzyme is a tetramer with, pseudofour-fold rotational symmetry. The subunits are six-stranded, beta-barrels capped by small alpha-helices at each end. The active sites, are located between adjacent subunits. The electron density provides, evidence for catalytic pyruvoyl groups at three active sites and an ester, at the fourth. The ester is an intermediate in the autocatalytic, self-processing leading to formation of the pyruvoyl group. This, unprecedented structure provides novel insights into the general, phenomenon of protein processing.

About this Structure

1AW8 is a [Protein complex] structure of sequences from [Escherichia coli]. Active as [Aspartate 1-decarboxylase], with EC number [4.1.1.11]. Structure known Active Site: NUL. Full crystallographic information is available from [OCA].

Reference

Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing., Albert A, Dhanaraj V, Genschel U, Khan G, Ramjee MK, Pulido R, Sibanda BL, von Delft F, Witty M, Blundell TL, Smith AG, Abell C, Nat Struct Biol. 1998 Apr;5(4):289-93. PMID:9546220

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