1lu3: Difference between revisions
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[[Image:1lu3.gif|left|200px]] | [[Image:1lu3.gif|left|200px]] | ||
'''Separate Fitting of the Anticodon Loop Region of tRNA (nucleotide 26-42) in the Low Resolution Cryo-EM Map of an EF-Tu Ternary Complex (GDP and Kirromycin) Bound to E. coli 70S Ribosome''' | {{Structure | ||
|PDB= 1lu3 |SIZE=350|CAPTION= <scene name='initialview01'>1lu3</scene>, resolution 16.8Å | |||
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|LIGAND= | |||
|ACTIVITY= | |||
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'''Separate Fitting of the Anticodon Loop Region of tRNA (nucleotide 26-42) in the Low Resolution Cryo-EM Map of an EF-Tu Ternary Complex (GDP and Kirromycin) Bound to E. coli 70S Ribosome''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1LU3 is a [ | 1LU3 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LU3 OCA]. | ||
==Reference== | ==Reference== | ||
Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process., Valle M, Sengupta J, Swami NK, Grassucci RA, Burkhardt N, Nierhaus KH, Agrawal RK, Frank J, EMBO J. 2002 Jul 1;21(13):3557-67. PMID:[http:// | Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process., Valle M, Sengupta J, Swami NK, Grassucci RA, Burkhardt N, Nierhaus KH, Agrawal RK, Frank J, EMBO J. 2002 Jul 1;21(13):3557-67. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12093756 12093756] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
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[[Category: trna]] | [[Category: trna]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:35:14 2008'' | ||
Revision as of 13:35, 20 March 2008
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Separate Fitting of the Anticodon Loop Region of tRNA (nucleotide 26-42) in the Low Resolution Cryo-EM Map of an EF-Tu Ternary Complex (GDP and Kirromycin) Bound to E. coli 70S Ribosome
OverviewOverview
During the elongation cycle of protein biosynthesis, the specific amino acid coded for by the mRNA is delivered by a complex that is comprised of the cognate aminoacyl-tRNA, elongation factor Tu and GTP. As this ternary complex binds to the ribosome, the anticodon end of the tRNA reaches the decoding center in the 30S subunit. Here we present the cryo- electron microscopy (EM) study of an Escherichia coli 70S ribosome-bound ternary complex stalled with an antibiotic, kirromycin. In the cryo-EM map the anticodon arm of the tRNA presents a new conformation that appears to facilitate the initial codon-anticodon interaction. Furthermore, the elbow region of the tRNA is seen to contact the GTPase-associated center on the 50S subunit of the ribosome, suggesting an active role of the tRNA in the transmission of the signal prompting the GTP hydrolysis upon codon recognition.
About this StructureAbout this Structure
1LU3 is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process., Valle M, Sengupta J, Swami NK, Grassucci RA, Burkhardt N, Nierhaus KH, Agrawal RK, Frank J, EMBO J. 2002 Jul 1;21(13):3557-67. PMID:12093756
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