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3me0
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3me0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3me0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3me0 RCSB], [http://www.ebi.ac.uk/pdbsum/3me0 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3me0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3me0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3me0 RCSB], [http://www.ebi.ac.uk/pdbsum/3me0 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://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> | ||
Revision as of 11:40, 25 December 2014
Structure of the E. coli chaperone PAPD in complex with the pilin domain of the PapGII adhesin
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