2nsa: Difference between revisions
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==Structures of and interactions between domains of trigger factor from Themotoga maritim== | ==Structures of and interactions between domains of trigger factor from Themotoga maritim== | ||
<StructureSection load='2nsa' size='340' side='right' caption='[[2nsa]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='2nsa' size='340' side='right'caption='[[2nsa]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2nsa]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2nsa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NSA FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tig ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tig ([https://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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2nsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nsa OCA], [https://pdbe.org/2nsa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nsa RCSB], [https://www.ebi.ac.uk/pdbsum/2nsa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nsa ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/TIG_THEMA 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). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Atcc 43589]] | [[Category: Atcc 43589]] | ||
[[Category: Large Structures]] | |||
[[Category: Hendrickson, W A]] | [[Category: Hendrickson, W A]] | ||
[[Category: Martinez-Hackert, E]] | [[Category: Martinez-Hackert, E]] | ||
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
Revision as of 18:50, 8 June 2021
Structures of and interactions between domains of trigger factor from Themotoga maritimStructures of and interactions between domains of trigger factor from Themotoga maritim
Structural highlights
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). 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 PubMedTrigger factor (TF) is a eubacterial chaperone that associates with ribosomes at the peptide-exit tunnel and also occurs in excess free in the cytosol. TF is a three-domain protein that appears to exist in a dynamic equilibrium of oligomerization states and interdomain conformations. X-ray crystallography and chemical cross-linking were used to study the roles of the N- and C-terminal domains of Thermotoga maritima TF in TF oligomerization and chaperone activity. The structural conservation of both the N- and C-terminal TF domains was unambiguously established. The biochemical and crystallographic data reveal a tendency for these domains to partake in diverse and apparently nonspecific protein-protein interactions. It is found that the T. maritima and Escherichia coli TF surfaces lack evident exposed hydrophobic patches. Taken together, these data suggest that TF chaperones could interact with nascent proteins via hydrophilic surfaces. Structures of and interactions between domains of trigger factor from Thermotoga maritima.,Martinez-Hackert E, Hendrickson WA Acta Crystallogr D Biol Crystallogr. 2007 Apr;63(Pt 4):536-47. Epub 2007, Mar 16. PMID:17372359[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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