2j2z

From Proteopedia

(Difference between revisions)

Revision as of 08:00, 19 January 2022

X-Ray Structure of the Chaperone PapD in complex with the Pilus terminator subunit PapH at 2.3 Angstrom resolution

Structural highlights

2j2z is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1n0l, 1pdk, 1qpp, 1qpx, 3dpa
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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. [PAPH_ECOLX] Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs. PapH seems to anchor the pilus to the bacterial cell. In addition the stoichiometric relationship between PapH and PapA determines the pilus length.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

P pili are important adhesive fibres that are assembled by the conserved chaperone-usher pathway. During pilus assembly, the subunits are incorporated into the growing fibre by the donor-strand exchange mechanism, whereby the beta-strand of the chaperone, which complements the incomplete immunoglobulin fold of each subunit, is displaced by the amino-terminal extension of an incoming subunit in a zip-in-zip-out exchange process that is initiated at the P5 pocket, an exposed hydrophobic pocket in the groove of the subunit. In vivo, termination of P pilus growth requires a specialized subunit, PapH. Here, we show that PapH is incorporated at the base of the growing pilus, where it is unable to undergo donor-strand exchange. This inability is not due to a stronger PapD-PapH interaction, but to a lack of a P5 initiator pocket in the PapH structure, suggesting that PapH terminates pilus growth because it is lacking the initiation point by which donor-strand exchange proceeds.

Molecular mechanism of P pilus termination in uropathogenic Escherichia coli.,Verger D, Miller E, Remaut H, Waksman G, Hultgren S EMBO Rep. 2006 Dec;7(12):1228-32. Epub 2006 Nov 3. PMID:17082819^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Verger D, Miller E, Remaut H, Waksman G, Hultgren S. Molecular mechanism of P pilus termination in uropathogenic Escherichia coli. EMBO Rep. 2006 Dec;7(12):1228-32. Epub 2006 Nov 3. PMID:17082819

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2j2z"

@@ Line 3: / Line 3: @@
 <StructureSection load='2j2z' size='340' side='right'caption='[[2j2z]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2j2z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J2Z OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2J2Z FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2j2z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J2Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J2Z FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1n0l|1n0l]], [[1pdk|1pdk]], [[1qpp|1qpp]], [[1qpx|1qpx]], [[3dpa|3dpa]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1n0l|1n0l]], [[1pdk|1pdk]], [[1qpp|1qpp]], [[1qpx|1qpx]], [[3dpa|3dpa]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2j2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j2z OCA], [http://pdbe.org/2j2z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j2z RCSB], [http://www.ebi.ac.uk/pdbsum/2j2z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2j2z ProSAT]</span></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=2j2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j2z OCA], [https://pdbe.org/2j2z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j2z RCSB], [https://www.ebi.ac.uk/pdbsum/2j2z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j2z ProSAT]</span></td></tr>
 </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. [[http://www.uniprot.org/uniprot/PAPH_ECOLX PAPH_ECOLX]] Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs.  PapH seems to anchor the pilus to the bacterial cell. In addition the stoichiometric relationship between PapH and PapA determines the pilus length.
+[[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. [[https://www.uniprot.org/uniprot/PAPH_ECOLX PAPH_ECOLX]] Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs.  PapH seems to anchor the pilus to the bacterial cell. In addition the stoichiometric relationship between PapH and PapA determines the pilus length.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2j2z

From Proteopedia

Revision as of 08:00, 19 January 2022

X-Ray Structure of the Chaperone PapD in complex with the Pilus terminator subunit PapH at 2.3 Angstrom resolution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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