12as

From Proteopedia

Revision as of 06:21, 30 October 2007

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 [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

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