11as
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(New page: 200px<br /><applet load="11as" size="450" color="white" frame="true" align="right" spinBox="true" caption="11as, resolution 2.5Å" /> '''ASPARAGINE SYNTHETASE...)
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Revision as of 08:18, 20 November 2007
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ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE
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
11AS is a Single protein structure of sequence from Escherichia coli with ASN as ligand. Active as Aspartate--ammonia ligase, with EC number 6.3.1.1 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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