1qpx

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{{Seed}}
 
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[[Image:1qpx.png|left|200px]]
 
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==CRYSTAL STRUCTURES OF SELF-CAPPING PAPD CHAPERONE HOMODIMERS==
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The line below this paragraph, containing "STRUCTURE_1qpx", creates the "Structure Box" on the page.
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<StructureSection load='1qpx' size='340' side='right'caption='[[1qpx]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1qpx]] 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=1QPX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QPX FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qpx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qpx OCA], [https://pdbe.org/1qpx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qpx RCSB], [https://www.ebi.ac.uk/pdbsum/1qpx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qpx ProSAT]</span></td></tr>
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{{STRUCTURE_1qpx| PDB=1qpx | SCENE= }}
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qp/1qpx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qpx ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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PapD is an immunoglobulin-like chaperone that mediates the assembly of P pili in uropathogenic strains of Escherichia coli. It binds and caps interactive surfaces on pilus subunits to prevent their premature associations in the periplasm. We elucidated the structural basis of a mechanism whereby PapD also interacts with itself, capping its own subunit binding surface. Crystal structures of dimeric forms of PapD revealed that this self-capping mechanism involves a rearrangement and ordering of the C2-D2 and F1-G1 loops upon dimerization which might ensure that a stable dimer is not formed in solution in spite of a relatively large dimer interface. An analysis of site directed mutations revealed that chaperone dimerization requires the same surface that is otherwise used to bind subunits.
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===CRYSTAL STRUCTURES OF SELF-CAPPING PAPD CHAPERONE HOMODIMERS===
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Structural basis of chaperone self-capping in P pilus biogenesis.,Hung DL, Pinkner JS, Knight SD, Hultgren SJ Proc Natl Acad Sci U S A. 1999 Jul 6;96(14):8178-83. PMID:10393968<ref>PMID:10393968</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_10393968}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1qpx" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 10393968 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10393968}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1QPX is a 2 chains structure of sequences 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=1QPX OCA].
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==Reference==
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<ref group="xtra">PMID:10393968</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Hultgren, S J.]]
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[[Category: Large Structures]]
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[[Category: Hung, D L.]]
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[[Category: Hultgren SJ]]
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[[Category: Knight, S D.]]
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[[Category: Hung DL]]
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[[Category: Pinkner, J S.]]
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[[Category: Knight SD]]
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[[Category: Beta barrel]]
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[[Category: Pinkner JS]]
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[[Category: Chaperone]]
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[[Category: Immunoglobulin fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 11:55:59 2009''
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Current revision

CRYSTAL STRUCTURES OF SELF-CAPPING PAPD CHAPERONE HOMODIMERS

PDB ID 1qpx

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