Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing.

Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing.

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 adjacen...

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Bibliographic Details
Main Authors: Albert, A, Dhanaraj, V, Genschel, U, Khan, G, Ramjee, M, Pulido, R, Sibanda, B, von Delft, F, Witty, M, Blundell, T, Smith, A, Abell, C
Format: Journal article
Language:English
Published: 1998
Description
Summary: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.

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