3gty: Difference between revisions
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[[Image:3gty.png|left|200px]] | |||
[[Image:3gty. | |||
{{STRUCTURE_3gty| PDB=3gty | SCENE= }} | {{STRUCTURE_3gty| PDB=3gty | SCENE= }} | ||
===Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone=== | ===Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone=== | ||
{{ABSTRACT_PUBMED_19737520}} | {{ABSTRACT_PUBMED_19737520}} | ||
==About this Structure== | ==About this Structure== | ||
[[3gty]] is a 2 chain structure of [[Ribosomal protein S7]] with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GTY OCA]. | |||
==See Also== | |||
*[[Ribosomal protein S7|Ribosomal protein S7]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:019737520</ref><references group="xtra"/> | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
[[Category: Hendrickson, W A.]] | [[Category: Hendrickson, W A.]] | ||
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[[Category: Chaperone]] | [[Category: Chaperone]] | ||
[[Category: Chaperone-client complex]] | [[Category: Chaperone-client complex]] | ||
[[Category: Chaperone | [[Category: Chaperone-ribosomal protein complex]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
[[Category: Ribonucleoprotein]] | [[Category: Ribonucleoprotein]] | ||
| Line 39: | Line 30: | ||
[[Category: Rrna-binding]] | [[Category: Rrna-binding]] | ||
[[Category: Trna-binding]] | [[Category: Trna-binding]] | ||
Revision as of 20:53, 25 July 2012
Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone
Template:ABSTRACT PUBMED 19737520
About this Structure
3gty is a 2 chain structure of Ribosomal protein S7 with sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
See Also
Reference
- Martinez-Hackert E, Hendrickson WA. Promiscuous substrate recognition in folding and assembly activities of the trigger factor chaperone. Cell. 2009 Sep 4;138(5):923-34. PMID:19737520 doi:10.1016/j.cell.2009.07.044