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3dpa
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(Difference between revisions)
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</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=3dpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dpa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dpa RCSB], [http://www.ebi.ac.uk/pdbsum/3dpa PDBsum]</span></td></tr> | </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=3dpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dpa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dpa RCSB], [http://www.ebi.ac.uk/pdbsum/3dpa 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. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 07:15, 25 December 2014
CRYSTAL STRUCTURE OF CHAPERONE PROTEIN PAPD REVEALS AN IMMUNOGLOBULIN FOLD
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