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1n0v

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(New page: 200px<br /> <applet load="1n0v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n0v, resolution 2.85&Aring;" /> '''Crystal structure o...)
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'''Crystal structure of elongation factor 2'''<br />
'''Crystal structure of elongation factor 2'''<br />
==Overview==
==Overview==
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Two crystal structures of yeast translation elongation factor 2 (eEF2), were determined: the apo form at 2.9 A resolution and eEF2 in the presence, of the translocation inhibitor sordarin at 2.1 A resolution. The overall, conformation of apo eEF2 is similar to that of its prokaryotic homolog, elongation factor G (EF-G) in complex with GDP. Upon sordarin binding, the, three tRNA-mimicking C-terminal domains undergo substantial conformational, changes, while the three N-terminal domains containing the, nucleotide-binding site form an almost rigid unit. The conformation of, eEF2 in complex with sordarin is entirely different from known, conformations observed in crystal structures of EF-G or from cryo-EM, studies of EF-G-70S complexes. The domain rearrangements induced by, sordarin binding and the highly ordered drug-binding site observed in the, eEF2-sordarin structure provide a high-resolution structural basis for the, mechanism of sordarin inhibition. The two structures also emphasize the, dynamic nature of the ribosomal translocase.
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Two crystal structures of yeast translation elongation factor 2 (eEF2) were determined: the apo form at 2.9 A resolution and eEF2 in the presence of the translocation inhibitor sordarin at 2.1 A resolution. The overall conformation of apo eEF2 is similar to that of its prokaryotic homolog elongation factor G (EF-G) in complex with GDP. Upon sordarin binding, the three tRNA-mimicking C-terminal domains undergo substantial conformational changes, while the three N-terminal domains containing the nucleotide-binding site form an almost rigid unit. The conformation of eEF2 in complex with sordarin is entirely different from known conformations observed in crystal structures of EF-G or from cryo-EM studies of EF-G-70S complexes. The domain rearrangements induced by sordarin binding and the highly ordered drug-binding site observed in the eEF2-sordarin structure provide a high-resolution structural basis for the mechanism of sordarin inhibition. The two structures also emphasize the dynamic nature of the ribosomal translocase.
==About this Structure==
==About this Structure==
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1N0V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. The following page contains interesting information on the relation of 1N0V with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb81_1.html Elongation Factors]]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N0V OCA].
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1N0V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. The following page contains interesting information on the relation of 1N0V with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb81_1.html Elongation Factors]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N0V OCA].
==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Andersen, G.R.]]
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[[Category: Andersen, G R.]]
[[Category: Carr-Schmid, A.]]
[[Category: Carr-Schmid, A.]]
[[Category: Joergensen, R.]]
[[Category: Joergensen, R.]]
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[[Category: Kinzy, T.G.]]
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[[Category: Kinzy, T G.]]
[[Category: Nissen, P.]]
[[Category: Nissen, P.]]
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[[Category: Ortiz, P.A.]]
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[[Category: Ortiz, P A.]]
[[Category: g-protein cis-proline]]
[[Category: g-protein cis-proline]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:04:03 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:01 2008''

Revision as of 12:01, 21 February 2008


1n0v, resolution 2.85Å

Drag the structure with the mouse to rotate

Crystal structure of elongation factor 2

Overview

Two crystal structures of yeast translation elongation factor 2 (eEF2) were determined: the apo form at 2.9 A resolution and eEF2 in the presence of the translocation inhibitor sordarin at 2.1 A resolution. The overall conformation of apo eEF2 is similar to that of its prokaryotic homolog elongation factor G (EF-G) in complex with GDP. Upon sordarin binding, the three tRNA-mimicking C-terminal domains undergo substantial conformational changes, while the three N-terminal domains containing the nucleotide-binding site form an almost rigid unit. The conformation of eEF2 in complex with sordarin is entirely different from known conformations observed in crystal structures of EF-G or from cryo-EM studies of EF-G-70S complexes. The domain rearrangements induced by sordarin binding and the highly ordered drug-binding site observed in the eEF2-sordarin structure provide a high-resolution structural basis for the mechanism of sordarin inhibition. The two structures also emphasize the dynamic nature of the ribosomal translocase.

About this Structure

1N0V is a Single protein structure of sequence from Saccharomyces cerevisiae. The following page contains interesting information on the relation of 1N0V with [Elongation Factors]. Full crystallographic information is available from OCA.

Reference

Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase., Jorgensen R, Ortiz PA, Carr-Schmid A, Nissen P, Kinzy TG, Andersen GR, Nat Struct Biol. 2003 May;10(5):379-85. PMID:12692531

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