3gu0: Difference between revisions

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{{Seed}}
[[Image:3gu0.jpg|left|200px]]


<!--
==Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone==
The line below this paragraph, containing "STRUCTURE_3gu0", creates the "Structure Box" on the page.
<StructureSection load='3gu0' size='340' side='right'caption='[[3gu0]], [[Resolution|resolution]] 3.50&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'>[[3gu0]] is a 1 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=3GU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GU0 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]] 3.5&#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=3gu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gu0 OCA], [https://pdbe.org/3gu0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gu0 RCSB], [https://www.ebi.ac.uk/pdbsum/3gu0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gu0 ProSAT]</span></td></tr>
{{STRUCTURE_3gu0|  PDB=3gu0  |  SCENE=  }}
</table>
 
== Function ==
===Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone===
[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>
The line below this paragraph, {{ABSTRACT_PUBMED_19737520}}, adds the Publication Abstract to the page
  <jmolCheckbox>
(as it appears on PubMed at http://www.pubmed.gov), where 19737520 is the PubMed ID number.
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gu/3gu0_consurf.spt"</scriptWhenChecked>
-->
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
{{ABSTRACT_PUBMED_19737520}}
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
==About this Structure==
</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=3gu0 ConSurf].
3GU0 is a 1 chain structure of 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=3GU0 OCA].  
<div style="clear:both"></div>
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:19737520</ref><references group="xtra"/>
[[Category: Large Structures]]
[[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: Isomerase]]
[[Category: Molecular chaperone]]
[[Category: Rotamase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Dec 24 07:28:06 2009''

Latest revision as of 09:56, 21 February 2024

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

3gu0, resolution 3.50Å

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