1eqr
From Proteopedia
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CRYSTAL STRUCTURE OF FREE ASPARTYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI
Overview
The crystal structure of aspartyl-tRNA synthetase from Escherichia coli, has been determined to a resolution of 2.7 A. The structure is compared to, the same enzyme co-crystallized with tRNA(Asp) and containing aspartyl, adenylate or ATP. The asymmetric unit contains three monomers of the, enzyme. While most parts of the protein show no significant differences in, the three monomers, a few regions cannot be superimposed. Those regions, are characterized by a high B-factor, and consist mostly of loops that, make contacts with the tRNA in the complexes. The flexibility of the, protein is seen at a global level, by the observation of a 10 to 15, degrees rotation of the N-terminal and insertion domains upon tRNA, binding, and at the level of the individual amino acid residues, by, main-chain and side-chain rearrangements. In contrast to these induced-fit, conformational changes, a few residues essential for the tRNA anticodon or, aspartyl-adenylate recognition exist in a predefined conformation, ensured, by specific interactions within the protein.
About this Structure
1EQR is a Single protein structure of sequence from Escherichia coli with MG as ligand. Active as Aspartate--tRNA ligase, with EC number 6.1.1.12 Full crystallographic information is available from OCA.
Reference
Aspartyl tRNA-synthetase from Escherichia coli: flexibility and adaptability to the substrates., Rees B, Webster G, Delarue M, Boeglin M, Moras D, J Mol Biol. 2000 Jun 23;299(5):1157-64. PMID:10873442
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