3me0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 8: Line 8:
<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

3me0, resolution 2.03Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools