3gty

From Proteopedia

(Difference between revisions)

Revision as of 07:13, 1 November 2017

Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone

Structural highlights

3gty is a 2 chain structure with sequence from Atcc 43589. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2nsc, 2nsb, 2nsa, 3gu0
Gene:	tig, TM_0694 (ATCC 43589), rpsG, TM_1504 (ATCC 43589)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TIG_THEMA] Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity). [RS7_THEMA] One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Trigger factor (TF) is a molecular chaperone that binds to bacterial ribosomes where it contacts emerging nascent chains, but TF is also abundant free in the cytosol where its activity is less well characterized. In vitro studies show that TF promotes protein refolding. We find here that ribosome-free TF stably associates with and rescues from misfolding a large repertoire of full-length proteins. We identify over 170 members of this cytosolic Escherichia coli TF substrate proteome, including ribosomal protein S7. We analyzed the biochemical properties of a TF:S7 complex from Thermotoga maritima and determined its crystal structure. Thereby, we obtained an atomic-level picture of a promiscuous chaperone in complex with a physiological substrate protein. The structure of the complex reveals the molecular basis of substrate recognition by TF, indicates how TF could accelerate protein folding, and suggests a role for TF in the biogenesis of protein complexes.

Promiscuous substrate recognition in folding and assembly activities of the trigger factor chaperone.,Martinez-Hackert E, Hendrickson WA Cell. 2009 Sep 4;138(5):923-34. PMID:19737520^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3gty"

@@ Line 1: / Line 1: @@
 ==Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone==
 <StructureSection load='3gty' size='340' side='right' caption='[[3gty]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2nsc|2nsc]], [[2nsb|2nsb]], [[2nsa|2nsa]], [[3gu0|3gu0]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tig, TM_0694 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589]), rpsG, TM_1504 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3gty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gty OCA], [http://pdbe.org/3gty PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gty RCSB], [http://www.ebi.ac.uk/pdbsum/3gty PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3gty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gty OCA], [http://pdbe.org/3gty PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gty RCSB], [http://www.ebi.ac.uk/pdbsum/3gty PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3gty ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 3gty" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Ribosomal protein S7|Ribosomal protein S7]]
 == References ==
 <references/>

3gty

From Proteopedia

Revision as of 07:13, 1 November 2017

Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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