1pdk: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1pdk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PDK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PDK FirstGlance]. <br> | <table><tr><td colspan='2'>[[1pdk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PDK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PDK FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pdk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pdk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pdk RCSB], [http://www.ebi.ac.uk/pdbsum/1pdk 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=1pdk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pdk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pdk RCSB], [http://www.ebi.ac.uk/pdbsum/1pdk 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. [[http://www.uniprot.org/uniprot/PAPK_ECOLX PAPK_ECOLX]] Adapter that links the pilus rod to the base of the tip fibrillum. Regulates the length of the tip fibrillum and joins it to the pilus rod. Pili are polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, and enable bacteria to colonize the epithelium of specific host organs. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Fuetterer, K | [[Category: Fuetterer, K]] | ||
[[Category: Hultgren, S J | [[Category: Hultgren, S J]] | ||
[[Category: Sauer, F G | [[Category: Sauer, F G]] | ||
[[Category: Waksman, G | [[Category: Waksman, G]] | ||
[[Category: Bacterial adhesion]] | [[Category: Bacterial adhesion]] | ||
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
[[Category: Pilus]] | [[Category: Pilus]] | ||
Revision as of 13:31, 25 December 2014
PAPD-PAPK CHAPERONE-PILUS SUBUNIT COMPLEX FROM E.COLI P PILUSPAPD-PAPK CHAPERONE-PILUS SUBUNIT COMPLEX FROM E.COLI P PILUS
Structural highlights
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. [PAPK_ECOLX] Adapter that links the pilus rod to the base of the tip fibrillum. Regulates the length of the tip fibrillum and joins it to the pilus rod. Pili are polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, and enable bacteria to colonize the epithelium of specific host organs. 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 PubMedMany Gram-negative pathogens assemble architecturally and functionally diverse adhesive pili on their surfaces by the chaperone-usher pathway. Immunoglobulin-like periplasmic chaperones escort pilus subunits to the usher, a large protein complex that facilitates the translocation and assembly of subunits across the outer membrane. The crystal structure of the PapD-PapK chaperone-subunit complex, determined at 2.4 angstrom resolution, reveals that the chaperone functions by donating its G(1) beta strand to complete the immunoglobulin-like fold of the subunit via a mechanism termed donor strand complementation. The structure of the PapD-PapK complex also suggests that during pilus biogenesis, every subunit completes the immunoglobulin-like fold of its neighboring subunit via a mechanism termed donor strand exchange. Structural basis of chaperone function and pilus biogenesis.,Sauer FG, Futterer K, Pinkner JS, Dodson KW, Hultgren SJ, Waksman G Science. 1999 Aug 13;285(5430):1058-61. PMID:10446050[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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