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

Abstract:

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 ...

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Publication status:
Published

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Publisher copy:
10.1038/nsb0498-289

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Journal:
Nature structural biology
Volume:
5
Issue:
4
Pages:
289-293
Publication date:
1998-04-05
DOI:
ISSN:
1072-8368
URN:
uuid:1eae8b3a-bde7-4dee-ae69-2b2b584fc69a
Source identifiers:
36171
Local pid:
pubs:36171

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