1eqr

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{{Seed}}
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{{STRUCTURE_1eqr| PDB=1eqr | SCENE= }}
{{STRUCTURE_1eqr| PDB=1eqr | SCENE= }}
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'''CRYSTAL STRUCTURE OF FREE ASPARTYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI'''
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===CRYSTAL STRUCTURE OF FREE ASPARTYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10873442 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10873442}}
==About this Structure==
==About this Structure==
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:25:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 01:43:55 2008''

Revision as of 22:43, 30 June 2008

Image:1eqr.png

Template:STRUCTURE 1eqr

CRYSTAL STRUCTURE OF FREE ASPARTYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI

Template:ABSTRACT PUBMED 10873442

About this Structure

1EQR is a Single protein structure of sequence from Escherichia coli. 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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