3me0: Difference between revisions
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==Structure of the E. coli chaperone PAPD in complex with the pilin domain of the PapGII adhesin== | ==Structure of the E. coli chaperone PAPD in complex with the pilin domain of the PapGII adhesin== | ||
<StructureSection load='3me0' size='340' side='right' caption='[[3me0]], [[Resolution|resolution]] 2.03Å' scene=''> | <StructureSection load='3me0' size='340' side='right'caption='[[3me0]], [[Resolution|resolution]] 2.03Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3me0]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3me0]] is a 2 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=3ME0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ME0 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]] 2.03Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3me0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3me0 OCA], [https://pdbe.org/3me0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3me0 RCSB], [https://www.ebi.ac.uk/pdbsum/3me0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3me0 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/PAPD_ECOLX PAPD_ECOLX] Binds and caps interactive surfaces on pilus subunits to prevent them from participating in non-productive interactions. Facilitates the import of subunits into the periplasm. May facilitate subunit folding. Chaperone-subunit complexes are then targeted to the PapC outer membrane usher where the chaperone must uncap from the subunits. | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Dodson KW]] | ||
[[Category: | [[Category: Elam JS]] | ||
[[Category: | [[Category: Ford BA]] | ||
[[Category: | [[Category: Hultgren SJ]] | ||
[[Category: | [[Category: Pinkner JS]] | ||
Latest revision as of 08:47, 7 February 2024
Structure of the E. coli chaperone PAPD in complex with the pilin domain of the PapGII adhesin
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