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3vnu
From Proteopedia
(Difference between revisions)
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| - | [[Image:3vnu.jpg|left|200px]] | ||
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{{STRUCTURE_3vnu| PDB=3vnu | SCENE= }} | {{STRUCTURE_3vnu| PDB=3vnu | SCENE= }} | ||
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===Complex structure of viral RNA polymerase I=== | ===Complex structure of viral RNA polymerase I=== | ||
| + | {{ABSTRACT_PUBMED_22884418}} | ||
| + | ==Function== | ||
| + | [[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== | ||
| - | [[3vnu]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[3vnu]] is a 3 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=3VNU OCA]. |
| - | [[Category: | + | |
| + | ==Reference== | ||
| + | <ref group="xtra">PMID:022884418</ref><references group="xtra"/><references/> | ||
| + | [[Category: Synthetic construct]] | ||
[[Category: Takeshita, D.]] | [[Category: Takeshita, D.]] | ||
[[Category: Tomita, K.]] | [[Category: Tomita, K.]] | ||
Revision as of 05:06, 10 October 2013
Contents |
Complex structure of viral RNA polymerase I
Template:ABSTRACT PUBMED 22884418
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
3vnu is a 3 chain structure with sequence from Synthetic construct. Full crystallographic information is available from OCA.
Reference
- Takeshita D, Yamashita S, Tomita K. Mechanism for template-independent terminal adenylation activity of Qbeta replicase. Structure. 2012 Oct 10;20(10):1661-9. doi: 10.1016/j.str.2012.07.004. Epub 2012, Aug 9. PMID:22884418 doi:http://dx.doi.org/10.1016/j.str.2012.07.004
