1ser
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(New page: 200px<br /><applet load="1ser" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ser, resolution 2.900Å" /> '''THE 2.9 ANGSTROMS C...)
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Revision as of 00:12, 21 November 2007
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THE 2.9 ANGSTROMS CRYSTAL STRUCTURE OF T. THERMOPHILUS SERYL-TRNA SYNTHETASE COMPLEXED WITH TRNA SER
Overview
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.
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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