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New page: '''Unreleased structure''' The entry 3me0 is ON HOLD Authors: Ford, B.A., Elam, J.S., Dodson, K.W., Pinkner, J.S., Hultgren, S.J. Description: STRUCTURE OF THE E. COLI CHAPERONE PAPD I... |
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==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=''> | |||
== Structural highlights == | |||
<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='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='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> | ||
</table> | |||
== 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__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | |||
[[Category: Dodson KW]] | |||
[[Category: Elam JS]] | |||
[[Category: Ford BA]] | |||
[[Category: Hultgren SJ]] | |||
[[Category: Pinkner JS]] | |||
Latest revision as of 11:47, 7 February 2024
Structure of the E. coli chaperone PAPD in complex with the pilin domain of the PapGII adhesinStructure of the E. coli chaperone PAPD in complex with the pilin domain of the PapGII adhesin
Structural highlights
FunctionPAPD_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. |
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