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1ser

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{{STRUCTURE_1ser| PDB=1ser | SCENE= }}
{{STRUCTURE_1ser| PDB=1ser | SCENE= }}
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'''THE 2.9 ANGSTROMS CRYSTAL STRUCTURE OF T. THERMOPHILUS SERYL-TRNA SYNTHETASE COMPLEXED WITH TRNA SER'''
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===THE 2.9 ANGSTROMS CRYSTAL STRUCTURE OF T. THERMOPHILUS SERYL-TRNA SYNTHETASE COMPLEXED WITH TRNA SER===
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==Overview==
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The crystal structure of Thermus thermophilus seryl-transfer RNA synthetase, a class 2 aminoacyl-tRNA synthetase, complexed with a single tRNA(Ser) molecule was solved at 2.9 A resolution. The structure revealed how insertion of conserved base G20b from the D loop into the core of the tRNA determines the orientation of the long variable arm, which is a characteristic feature of most serine specific tRNAs. On tRNA binding, the antiparallel coiled-coil domain of one subunit of the synthetase makes contacts with the variable arm and T psi C loop of the tRNA and directs the acceptor stem of the tRNA into the active site of the other subunit. Specificity depends principally on recognition of the shape of tRNA(Ser) through backbone contacts and secondarily on sequence specific interactions.
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(as it appears on PubMed at http://www.pubmed.gov), where 8128220 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8128220}}
==About this Structure==
==About this Structure==
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[[Category: Yaremchuk, A.]]
[[Category: Yaremchuk, A.]]
[[Category: Protein-t-rna complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:36:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:59:50 2008''

Revision as of 06:59, 28 July 2008

Image:1ser.png

Template:STRUCTURE 1ser

THE 2.9 ANGSTROMS CRYSTAL STRUCTURE OF T. THERMOPHILUS SERYL-TRNA SYNTHETASE COMPLEXED WITH TRNA SER

Template:ABSTRACT PUBMED 8128220

About this Structure

1SER is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

The 2.9 A crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA(Ser)., Biou V, Yaremchuk A, Tukalo M, Cusack S, Science. 1994 Mar 11;263(5152):1404-10. PMID:8128220

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