12as
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 12AS is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with ASN and AMP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ | + | 12AS is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with ASN and AMP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Aspartate--ammonia_ligase Aspartate--ammonia ligase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.1 6.3.1.1]]. Structure known Active Sites: NU1 and NU2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=12AS OCA]]. |
==Reference== | ==Reference== | ||
Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase., Nakatsu T, Kato H, Oda J, Nat Struct Biol. 1998 Jan;5(1):15-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9437423 9437423] | Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase., Nakatsu T, Kato H, Oda J, Nat Struct Biol. 1998 Jan;5(1):15-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9437423 9437423] | ||
| + | [[Category: Aspartate--ammonia ligase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: nitrogen fixation]] | [[Category: nitrogen fixation]] | ||
| - | ''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 10:20:20 2007'' |
Revision as of 08:15, 30 October 2007
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ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE AND AMP
Overview
The crystal structure of E. coli asparagine synthetase has been determined, by X-ray diffraction analysis at 2.5 A resolution. The overall structure, of the enzyme is remarkably similar to that of the catalytic domain of, yeast aspartyl-tRNA synthetase despite low sequence similarity. These, enzymes have a common reaction mechanism that implies the formation of an, aminoacyl-adenylate intermediate. The active site architecture and most of, the catalytic residues are also conserved in both enzymes. These proteins, have probably evolved from a common ancestor even though their sequence, similarities are small. The functional and structural similarities of both, enzymes suggest that new enzymatic activities would generally follow the, recruitment of a protein catalyzing a similar chemical ... [(full description)]
About this Structure
12AS is a [Single protein] structure of sequence from [Escherichia coli] with ASN and AMP as [ligands]. Active as [Aspartate--ammonia ligase], with EC number [6.3.1.1]. Structure known Active Sites: NU1 and NU2. Full crystallographic information is available from [OCA].
Reference
Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase., Nakatsu T, Kato H, Oda J, Nat Struct Biol. 1998 Jan;5(1):15-9. PMID:9437423
Page seeded by OCA on Tue Oct 30 10:20:20 2007
