3f65
From Proteopedia
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==The F4 fimbrial chaperone FaeE does not self-cap its interactive surfaces== | ==The F4 fimbrial chaperone FaeE does not self-cap its interactive surfaces== | ||
- | <StructureSection load='3f65' size='340' side='right' caption='[[3f65]], [[Resolution|resolution]] 2.29Å' scene=''> | + | <StructureSection load='3f65' size='340' side='right'caption='[[3f65]], [[Resolution|resolution]] 2.29Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3f65]] is a 8 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3f65]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F65 FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.29Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=3f65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f65 OCA], [https://pdbe.org/3f65 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f65 RCSB], [https://www.ebi.ac.uk/pdbsum/3f65 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f65 ProSAT]</span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/FAEE_ECOLX FAEE_ECOLX] Mediates assembly of pili by forming soluble multimeric complexes with pili subunits as an intermediate step in the assembly process. This protein is involved in K88 pili assembly. Protects pilin protein from proteolytic degradation by DegP and from premature polymerization. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
- | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f6/3f65_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f6/3f65_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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=3f65 ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
+ | <div class="pdbe-citations 3f65" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Bouckaert J]] |
- | [[Category: | + | [[Category: Buts L]] |
- | [[Category: Greve | + | [[Category: De Greve H]] |
- | [[Category: | + | [[Category: Garcia-Pino A]] |
- | [[Category: Moonens | + | [[Category: Moonens K]] |
- | [[Category: | + | [[Category: Van Molle I]] |
- | [[Category: | + | [[Category: Wyns L]] |
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Current revision
The F4 fimbrial chaperone FaeE does not self-cap its interactive surfaces
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