1qpx

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(New page: 200px<br /><applet load="1qpx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qpx, resolution 2.4&Aring;" /> '''CRYSTAL STRUCTURES OF...)
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[[Image:1qpx.jpg|left|200px]]<br /><applet load="1qpx" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qpx, resolution 2.4&Aring;" />
 
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'''CRYSTAL STRUCTURES OF SELF-CAPPING PAPD CHAPERONE HOMODIMERS'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURES OF SELF-CAPPING PAPD CHAPERONE HOMODIMERS==
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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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<StructureSection load='1qpx' size='340' side='right'caption='[[1qpx]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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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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</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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</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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==About this Structure==
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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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1QPX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QPX OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10393968 10393968]
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</div>
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<div class="pdbe-citations 1qpx" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hultgren, S.J.]]
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[[Category: Hultgren SJ]]
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[[Category: Hung, D.L.]]
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[[Category: Hung DL]]
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[[Category: Knight, S.D.]]
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[[Category: Knight SD]]
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[[Category: Pinkner, J.S.]]
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[[Category: Pinkner JS]]
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[[Category: beta barrel]]
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[[Category: chaperone]]
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[[Category: immunoglobulin fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:52:44 2007''
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Current revision

CRYSTAL STRUCTURES OF SELF-CAPPING PAPD CHAPERONE HOMODIMERS

PDB ID 1qpx

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