1aw8
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1AW8 is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]]. Active as [[http://en.wikipedia.org/wiki/ | + | 1AW8 is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]]. Active as [[http://en.wikipedia.org/wiki/Aspartate_1-decarboxylase Aspartate 1-decarboxylase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.11 4.1.1.11]]. Structure known Active Site: NUL. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AW8 OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9546220 9546220] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9546220 9546220] | ||
| + | [[Category: Aspartate 1-decarboxylase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: protein self-processing]] | [[Category: protein self-processing]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:42:00 2007'' |
Revision as of 08:37, 30 October 2007
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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
Page seeded by OCA on Tue Oct 30 10:42:00 2007
Categories: Aspartate 1-decarboxylase | Escherichia coli | Protein complex | Abell, C. | Albert, A. | Blundell, T.L. | Dhanaraj, V. | Genschel, U. | Khan, G. | Pulido, R. | Ramjee, M.K. | Smith, A.G. | Sybanda, B.L. | Vondelf, F. | Witty, M. | Decarboxylase | Lyase | Pantothenate pathway | Protein self-processing
