2j2z: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(18 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2j2z.gif|left|200px]]<br />
<applet load="2j2z" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2j2z, resolution 2.3&Aring;" />
'''X-RAY STRUCTURE OF THE CHAPERONE PAPD IN COMPLEX WITH THE PILUS TERMINATOR SUBUNIT PAPH AT 2.3 ANGSTROM RESOLUTION'''<br />


==Overview==
==X-Ray Structure of the Chaperone PapD in complex with the Pilus terminator subunit PapH at 2.3 Angstrom resolution==
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.
<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 [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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='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 ==
[https://www.uniprot.org/uniprot/Q7ATU9_ECOLX Q7ATU9_ECOLX]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j2/2j2z_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2j2z ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==About this Structure==
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<ref>PMID:17082819</ref>
2J2Z is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 and CO as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J2Z OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17082819 17082819]
</div>
<div class="pdbe-citations 2j2z" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Pilin 3D structures|Pilin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Hultgren, S.]]
[[Category: Hultgren S]]
[[Category: Miller, E.]]
[[Category: Miller E]]
[[Category: Remaut, H.]]
[[Category: Remaut H]]
[[Category: Verger, D.]]
[[Category: Verger D]]
[[Category: Waksman, G.]]
[[Category: Waksman G]]
[[Category: CO]]
[[Category: SO4]]
[[Category: chaperone]]
[[Category: chaperone/ surface active protein complex]]
[[Category: fimbria]]
[[Category: immunoglobulin domain]]
[[Category: p5 pocket]]
[[Category: papd]]
[[Category: paph]]
[[Category: periplasmic]]
[[Category: pilus termination]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 18:23:49 2007''

Latest revision as of 09:12, 6 November 2024

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

2j2z, resolution 2.30Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA