11as

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{{STRUCTURE_11as| PDB=11as | SCENE= }}
{{STRUCTURE_11as| PDB=11as | SCENE= }}
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'''ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE'''
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===ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9437423 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9437423}}
==About this Structure==
==About this Structure==
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[[Category: Ligase]]
[[Category: Ligase]]
[[Category: Nitrogen fixation]]
[[Category: Nitrogen fixation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:24:35 2008''

Revision as of 12:24, 30 June 2008

Image:11as.png

Template:STRUCTURE 11as

ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE

Template:ABSTRACT PUBMED 9437423

About this Structure

11AS is a Single protein structure of sequence from Escherichia coli. 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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