1n32: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="1n32" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n32, resolution 3.00Å" /> '''Structure of the The...
 
No edit summary
Line 1: Line 1:
[[Image:1n32.gif|left|200px]]<br /><applet load="1n32" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1n32.gif|left|200px]]<br /><applet load="1n32" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1n32, resolution 3.00&Aring;" />
caption="1n32, resolution 3.00&Aring;" />
'''Structure of the Thermus thermophilus 30S ribosomal subunit bound to codon and near-cognate transfer RNA anticodon stem-loop mismatched at the first codon position at the a site with paromomycin'''<br />
'''Structure of the Thermus thermophilus 30S ribosomal subunit bound to codon and near-cognate transfer RNA anticodon stem-loop mismatched at the first codon position at the a site with paromomycin'''<br />


==Overview==
==Overview==
A structural and mechanistic explanation for the selection of tRNAs by the, ribosome has been elusive. Here, we report crystal structures of the 30S, ribosomal subunit with codon and near-cognate tRNA anticodon stem loops, bound at the decoding center and compare affinities of equivalent, complexes in solution. In ribosomal interactions with near-cognate tRNA, deviation from Watson-Crick geometry results in uncompensated desolvation, of hydrogen-bonding partners at the codon-anticodon minor groove. As a, result, the transition to a closed form of the 30S induced by cognate tRNA, is unfavorable for near-cognate tRNA unless paromomycin induces part of, the rearrangement. We conclude that stabilization of a closed 30S, conformation is required for tRNA selection, and thereby structurally, rationalize much previous data on translational fidelity.
A structural and mechanistic explanation for the selection of tRNAs by the ribosome has been elusive. Here, we report crystal structures of the 30S ribosomal subunit with codon and near-cognate tRNA anticodon stem loops bound at the decoding center and compare affinities of equivalent complexes in solution. In ribosomal interactions with near-cognate tRNA, deviation from Watson-Crick geometry results in uncompensated desolvation of hydrogen-bonding partners at the codon-anticodon minor groove. As a result, the transition to a closed form of the 30S induced by cognate tRNA is unfavorable for near-cognate tRNA unless paromomycin induces part of the rearrangement. We conclude that stabilization of a closed 30S conformation is required for tRNA selection, and thereby structurally rationalize much previous data on translational fidelity.


==About this Structure==
==About this Structure==
1N32 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with PAR, MG and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N32 OCA].  
1N32 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=PAR:'>PAR</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N32 OCA].  


==Reference==
==Reference==
Line 13: Line 13:
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[Category: IV, F.V.Murphy.]]
[[Category: IV, F V.Murphy.]]
[[Category: Ogle, J.M.]]
[[Category: Ogle, J M.]]
[[Category: Ramakrishnan, V.]]
[[Category: Ramakrishnan, V.]]
[[Category: Tarry, M.J.]]
[[Category: Tarry, M J.]]
[[Category: MG]]
[[Category: MG]]
[[Category: PAR]]
[[Category: PAR]]
Line 39: Line 39:
[[Category: wobble]]
[[Category: wobble]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:54:24 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:43 2008''

Revision as of 15:01, 21 February 2008

File:1n32.gif


1n32, resolution 3.00Å

Drag the structure with the mouse to rotate

Structure of the Thermus thermophilus 30S ribosomal subunit bound to codon and near-cognate transfer RNA anticodon stem-loop mismatched at the first codon position at the a site with paromomycin

OverviewOverview

A structural and mechanistic explanation for the selection of tRNAs by the ribosome has been elusive. Here, we report crystal structures of the 30S ribosomal subunit with codon and near-cognate tRNA anticodon stem loops bound at the decoding center and compare affinities of equivalent complexes in solution. In ribosomal interactions with near-cognate tRNA, deviation from Watson-Crick geometry results in uncompensated desolvation of hydrogen-bonding partners at the codon-anticodon minor groove. As a result, the transition to a closed form of the 30S induced by cognate tRNA is unfavorable for near-cognate tRNA unless paromomycin induces part of the rearrangement. We conclude that stabilization of a closed 30S conformation is required for tRNA selection, and thereby structurally rationalize much previous data on translational fidelity.

About this StructureAbout this Structure

1N32 is a Protein complex structure of sequences from Thermus thermophilus with , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Selection of tRNA by the ribosome requires a transition from an open to a closed form., Ogle JM, Murphy FV, Tarry MJ, Ramakrishnan V, Cell. 2002 Nov 27;111(5):721-32. PMID:12464183

Page seeded by OCA on Thu Feb 21 14:01:43 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA