PMID: 9546220Apr 18, 1998Paper

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

Nature Structural Biology
A AlbertChris Abell

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 leading to formation of the pyruvoyl group. This unprecedented structure provides novel insights into the general phenomenon of protein processing.

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Citations

Dec 10, 2009·Amino Acids·Shridhar Bale, Steven E Ealick
Aug 9, 2003·Structure·Narayanan ManojSteven E Ealick
Aug 17, 2002·Protein Expression and Purification·Sidharth ChopraAnand Ranganathan
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Sep 28, 2007·Natural Product Reports·Gemma L HollidayMartin J Warren
Sep 28, 2007·Natural Product Reports·Duncan E ScottChris Abell
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May 23, 2007·Molekuliarnaia biologiia·P L Starokadomskiĭ
Apr 5, 2014·Acta Crystallographica. Section D, Biological Crystallography·Michael E WebbChris Abell
Apr 17, 2012·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Michael E WebbChris Abell
Dec 17, 2003·The Plant Journal : for Cell and Molecular Biology·Harald H OttenhofAlison G Smith
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