1lu3: Difference between revisions

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[[Image:1lu3.gif|left|200px]]
[[Image:1lu3.gif|left|200px]]


{{Structure
<!--
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{{STRUCTURE_1lu3| PDB=1lu3  | SCENE= }}  
|RELATEDENTRY=[[1ls2|1LS2]], [[1efc|1EFC]], [[1ttt|1TTT]], [[1exm|1EXM]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lu3 OCA], [http://www.ebi.ac.uk/pdbsum/1lu3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lu3 RCSB]</span>
}}


'''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'''
'''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'''
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==About this Structure==
==About this Structure==
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].  
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://www.ncbi.nlm.nih.gov/pubmed/12093756 12093756]
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: Saccharomyces cerevisiae]]
[[Category: Agrawal, R K.]]
[[Category: Agrawal, R K.]]
[[Category: Burkhardt, N.]]
[[Category: Burkhardt, N.]]
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[[Category: Valle, M.]]
[[Category: Valle, M.]]
[[Category: 70s e coli ribosome]]
[[Category: 70s e coli ribosome]]
[[Category: conformational change]]
[[Category: Conformational change]]
[[Category: cryo-em]]
[[Category: Cryo-em]]
[[Category: ternary complex]]
[[Category: Ternary complex]]
[[Category: trna]]
[[Category: Trna]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:07:23 2008''

Revision as of 00:17, 3 May 2008

File:1lu3.gif

Template:STRUCTURE 1lu3

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

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 Page seeded by OCA on Sat May 3 00:17:23 2008

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