1ser: Difference between revisions
New page: left|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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[[Image:1ser.jpg|left|200px]]<br /><applet load="1ser" size=" | [[Image:1ser.jpg|left|200px]]<br /><applet load="1ser" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ser, resolution 2.900Å" /> | caption="1ser, resolution 2.900Å" /> | ||
'''THE 2.9 ANGSTROMS CRYSTAL STRUCTURE OF T. THERMOPHILUS SERYL-TRNA SYNTHETASE COMPLEXED WITH TRNA SER'''<br /> | '''THE 2.9 ANGSTROMS CRYSTAL STRUCTURE OF T. THERMOPHILUS SERYL-TRNA SYNTHETASE COMPLEXED WITH TRNA SER'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of Thermus thermophilus seryl-transfer RNA | 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== | ==About this Structure== | ||
1SER is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http:// | 1SER is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SER OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: protein-t-rna complex]] | [[Category: protein-t-rna complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:00:47 2008'' | ||
Revision as of 16:00, 21 February 2008
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THE 2.9 ANGSTROMS CRYSTAL STRUCTURE OF T. THERMOPHILUS SERYL-TRNA SYNTHETASE COMPLEXED WITH TRNA SER
OverviewOverview
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 StructureAbout this Structure
1SER is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
ReferenceReference
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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