1aw8

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{{STRUCTURE_1aw8| PDB=1aw8 | SCENE= }}
{{STRUCTURE_1aw8| PDB=1aw8 | SCENE= }}
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'''PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE'''
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===PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 9546220 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9546220}}
==About this Structure==
==About this Structure==
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[[Category: Pantothenate pathway]]
[[Category: Pantothenate pathway]]
[[Category: Protein self-processing]]
[[Category: Protein self-processing]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:44:06 2008''

Revision as of 14:44, 30 June 2008

Template:STRUCTURE 1aw8

PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE

Template:ABSTRACT PUBMED 9546220

About this Structure

1AW8 is a Protein complex structure of sequences from Escherichia coli. 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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