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| - | [[Image:1b23.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1b23| PDB=1b23 | SCENE= }} | | {{STRUCTURE_1b23| PDB=1b23 | SCENE= }} |
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| - | '''E. coli cysteinyl-tRNA and T. aquaticus elongation factor EF-TU:GTP ternary complex'''
| + | ===E. coli cysteinyl-tRNA and T. aquaticus elongation factor EF-TU:GTP ternary complex=== |
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| - | ==Overview==
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| - | BACKGROUND:. The translation elongation factor EF-Tu in its GTP-bound state forms a ternary complex with any aminoacylated tRNA (aa-tRNA), except initiator tRNA and selenocysteinyl-tRNA. This complex delivers aa-tRNA to the ribosomal A site during the elongation cycle of translation. The crystal structure of the yeast Phe-tRNAPhe ternary complex with Thermus aquaticus EF-Tu-GDPNP (Phe-TC) has previously been determined as one representative of this general yet highly discriminating complex formation. RESULTS: The ternary complex of Escherichia coli Cys-tRNACys and T. aquaticus EF-Tu-GDPNP (Cys-TC) has been solved and refined at 2.6 degrees resolution. Conserved and variable features of the aa-tRNA recognition and binding by EF-Tu-GTP have been revealed by comparison with the Phe-TC structure. New tertiary interactions are observed in the tRNACys structure. A 'kissing complex' is observed in the very close crystal packing arrangement. CONCLUSIONS: The recognition of Cys-tRNACys by EF-Tu-GDPNP is restricted to the aa-tRNA motif previously identified in Phe-TC and consists of the aminoacylated 3' end, the phosphorylated 5' end and one side of the acceptor stem and T stem. The aminoacyl bond is recognized somewhat differently, yet by the same primary motif in EF-Tu, which suggests that EF-Tu adapts to subtle variations in this moiety among all aa-tRNAs. New tertiary interactions revealed by the Cys-tRNACys structure, such as a protonated C16:C59 pyrimidine pair, a G15:G48 'Levitt pair' and an s4U8:A14:A46 base triple add to the generic understanding of tRNA structure from sequence. The structure of the 'kissing complex' shows a quasicontinuous helix with a distinct shape determined by the number of base pairs.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10368282}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10368282 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10368282}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Transfer rna]] | | [[Category: Transfer rna]] |
| | [[Category: Translation elongation factor]] | | [[Category: Translation elongation factor]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:57:56 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:03:41 2008'' |
Revision as of 15:03, 30 June 2008
Template:STRUCTURE 1b23
E. coli cysteinyl-tRNA and T. aquaticus elongation factor EF-TU:GTP ternary complex
Template:ABSTRACT PUBMED 10368282
About this Structure
1B23 is a Single protein structure of sequence from Escherichia coli and Thermus aquaticus. Full crystallographic information is available from OCA.
Reference
The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA., Nissen P, Thirup S, Kjeldgaard M, Nyborg J, Structure. 1999 Feb 15;7(2):143-56. PMID:10368282
Page seeded by OCA on Mon Jun 30 18:03:41 2008
