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12as
From Proteopedia
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| - | [[Image:12as.gif|left|200px]]<br /><applet load="12as" size=" | + | [[Image:12as.gif|left|200px]]<br /><applet load="12as" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="12as, resolution 2.2Å" /> | caption="12as, resolution 2.2Å" /> | ||
'''ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE AND AMP'''<br /> | '''ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE AND AMP'''<br /> | ||
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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/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] Known structural/functional Sites: <scene name='pdbsite=NU1:Amp Binding (Catalytic) Site (Chain A). Site Site_identi ...'>NU1</scene> and <scene name='pdbsite=NU2:Amp Binding (Catalytic) Site (Chain B)'>NU2</scene>. Full crystallographic information is available from [http:// | + | 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 <scene name='pdbligand=ASN:'>ASN</scene> and <scene name='pdbligand=AMP:'>AMP</scene> 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] Known structural/functional Sites: <scene name='pdbsite=NU1:Amp+Binding+(Catalytic)+Site+(Chain+A).+Site+Site_identi+...'>NU1</scene> and <scene name='pdbsite=NU2:Amp+Binding+(Catalytic)+Site+(Chain+B)'>NU2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=12AS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: nitrogen fixation]] | [[Category: nitrogen fixation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:28:27 2008'' |
Revision as of 07:28, 3 February 2008
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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 reaction.
About this Structure
12AS is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Aspartate--ammonia ligase, with EC number 6.3.1.1 Known structural/functional Sites: and . 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
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