2j2z
From Proteopedia
(Difference between revisions)
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<StructureSection load='2j2z' size='340' side='right' caption='[[2j2z]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='2j2z' size='340' side='right' caption='[[2j2z]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2j2z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2J2Z FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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">[[1n0l|1n0l]], [[1pdk|1pdk]], [[1qpp|1qpp]], [[1qpx|1qpx]], [[3dpa|3dpa]]</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=2j2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j2z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2j2z RCSB], [http://www.ebi.ac.uk/pdbsum/2j2z 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=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]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[http://www.uniprot.org/uniprot/ | + | [[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. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
+ | <div class="pdbe-citations 2j2z" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Bacillus coli migula 1895]] |
[[Category: Hultgren, S]] | [[Category: Hultgren, S]] | ||
[[Category: Miller, E]] | [[Category: Miller, E]] |
Revision as of 13:46, 10 September 2015
X-RAY STRUCTURE OF THE CHAPERONE PAPD IN COMPLEX WITH THE PILUS TERMINATOR SUBUNIT PAPH AT 2.3 ANGSTROM RESOLUTION
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Categories: Bacillus coli migula 1895 | Hultgren, S | Miller, E | Remaut, H | Verger, D | Waksman, G | Chaperone | Chaperone- surface active protein complex | Chaperone-surface active protein complex | Chaperone/surface active protein | Fimbria | Immunoglobulin domain | P5 pocket | Papd | Paph | Periplasmic | Pilus termination