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3agq

From Proteopedia

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m (Protected "3agq" [edit=sysop:move=sysop])
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[[Image:3agq.png|left|200px]]
 
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{{STRUCTURE_3agq| PDB=3agq | SCENE= }}
{{STRUCTURE_3agq| PDB=3agq | SCENE= }}
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===Structure of viral polymerase form II===
===Structure of viral polymerase form II===
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{{ABSTRACT_PUBMED_20798060}}
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{{ABSTRACT_PUBMED_020798060}}
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==Function==
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[[http://www.uniprot.org/uniprot/EFTS_ECO57 EFTS_ECO57]] Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (By similarity).
==About this Structure==
==About this Structure==
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[[3agq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AGQ OCA].
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[[3agq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AGQ OCA].
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[[Category: Synthetic construct]]
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==Reference==
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<ref group="xtra">PMID:020798060</ref><references group="xtra"/><references/>
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[[Category: Eco57]]
[[Category: Takeshita, D.]]
[[Category: Takeshita, D.]]
[[Category: Tomita, K.]]
[[Category: Tomita, K.]]

Revision as of 06:23, 29 January 2014

Template:STRUCTURE 3agq

Contents

Structure of viral polymerase form II

Template:ABSTRACT PUBMED 20798060

Function

[EFTS_ECO57] Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (By similarity).

About this Structure

3agq is a 1 chain structure with sequence from Eco57. Full crystallographic information is available from OCA.

Reference

  • Takeshita D, Tomita K. Assembly of Q{beta} viral RNA polymerase with host translational elongation factors EF-Tu and -Ts. Proc Natl Acad Sci U S A. 2010 Sep 7;107(36):15733-8. Epub 2010 Aug 23. PMID:20798060 doi:http://dx.doi.org/10.1073/pnas.1006559107

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