This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1n36

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1n36" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n36, resolution 3.65&Aring;" /> '''Structure of the The...)
Line 1: Line 1:
-
[[Image:1n36.gif|left|200px]]<br /><applet load="1n36" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1n36.gif|left|200px]]<br /><applet load="1n36" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1n36, resolution 3.65&Aring;" />
caption="1n36, resolution 3.65&Aring;" />
'''Structure of the Thermus thermophilus 30S ribosomal subunit in the presence of crystallographically disordered codon and near-cognate transfer RNA anticodon stem-loop mismatched at the second codon position'''<br />
'''Structure of the Thermus thermophilus 30S ribosomal subunit in the presence of crystallographically disordered codon and near-cognate transfer RNA anticodon stem-loop mismatched at the second codon position'''<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==
-
1N36 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 ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N36 OCA].
+
1N36 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=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N36 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: ZN]]
[[Category: ZN]]
[[Category: 30s ribosomal subunit]]
[[Category: 30s ribosomal subunit]]
Line 37: Line 37:
[[Category: wobble]]
[[Category: wobble]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:55:21 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:43 2008''

Revision as of 12:01, 21 February 2008


1n36, resolution 3.65Å

Drag the structure with the mouse to rotate

Structure of the Thermus thermophilus 30S ribosomal subunit in the presence of crystallographically disordered codon and near-cognate transfer RNA anticodon stem-loop mismatched at the second codon position

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.

About this Structure

1N36 is a Protein complex structure of sequences from Thermus thermophilus with as ligand. Full crystallographic information is available from OCA.

Reference

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?)

OCA

Personal tools