3gty: Difference between revisions

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[[Image:3gty.jpg|left|200px]]


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==Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone==
The line below this paragraph, containing "STRUCTURE_3gty", creates the "Structure Box" on the page.
<StructureSection load='3gty' size='340' side='right'caption='[[3gty]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3gty]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GTY FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
-->
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3gty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gty OCA], [https://pdbe.org/3gty PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gty RCSB], [https://www.ebi.ac.uk/pdbsum/3gty PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gty ProSAT]</span></td></tr>
{{STRUCTURE_3gty| PDB=3gty |  SCENE= }}
</table>
== 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gt/3gty_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3gty ConSurf].
<div style="clear:both"></div>


===Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone===
==See Also==
 
*[[Ribosomal protein S7|Ribosomal protein S7]]
 
__TOC__
==About this Structure==
</StructureSection>
3GTY is a 2 chains structure of sequences 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].
[[Category: Large Structures]]
 
==Reference==
<ref group="xtra">PMID:19737520</ref><references group="xtra"/>
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Hendrickson, W A.]]
[[Category: Hendrickson WA]]
[[Category: Martinez-Hackert, E.]]
[[Category: Martinez-Hackert E]]
[[Category: Cell cycle]]
[[Category: Cell division]]
[[Category: Chaperone]]
[[Category: Chaperone-client complex]]
[[Category: Chaperone/ribosomal protein complex]]
[[Category: Isomerase]]
[[Category: Ribonucleoprotein]]
[[Category: Ribosomal protein]]
[[Category: Rna-binding]]
[[Category: Rotamase]]
[[Category: Rrna-binding]]
[[Category: Trna-binding]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 23 09:58:21 2009''

Latest revision as of 09:56, 21 February 2024

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

3gty, resolution 3.40Å

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