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<StructureSection load='2co2' size='340' side='right'caption='[[2co2]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='2co2' size='340' side='right'caption='[[2co2]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2co2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_cholerae-suis"_smith_1894 "bacillus cholerae-suis" smith 1894]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CO2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CO2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2co2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CO2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CO2 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2cny|2cny]], [[2cnz|2cnz]], [[2co1|2co1]], [[2co3|2co3]], [[2co4|2co4]], [[2co6|2co6]], [[2co7|2co7]]</div></td></tr>
</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2co2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2co2 OCA], [https://pdbe.org/2co2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2co2 RCSB], [https://www.ebi.ac.uk/pdbsum/2co2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2co2 ProSAT]</span></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=2co2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2co2 OCA], [https://pdbe.org/2co2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2co2 RCSB], [https://www.ebi.ac.uk/pdbsum/2co2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2co2 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q8ZRK4_SALTY Q8ZRK4_SALTY]
Gram-negative pathogens commonly use the chaperone-usher pathway to assemble adhesive multisubunit fibers on their surface. In the periplasm, subunits are stabilized by a chaperone that donates a beta strand to complement the subunits' truncated immunoglobulin-like fold. Pilus assembly proceeds through a "donor-strand exchange" (DSE) mechanism whereby this complementary beta strand is replaced by the N-terminal extension (Nte) of an incoming pilus subunit. Using X-ray crystallography and real-time electrospray ionization mass spectrometry (ESI-MS), we demonstrate that DSE requires the formation of a transient ternary complex between the chaperone-subunit complex and the Nte of the next subunit to be assembled. The process is crucially dependent on an initiation site (the P5 pocket) needed to recruit the incoming Nte. The data also suggest a capping reaction displacing DSE toward product formation. These results support a zip-in-zip-out mechanism for DSE and a catalytic role for the usher, the molecular platform at which pili are assembled.


Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism.,Remaut H, Rose RJ, Hannan TJ, Hultgren SJ, Radford SE, Ashcroft AE, Waksman G Mol Cell. 2006 Jun 23;22(6):831-42. PMID:16793551<ref>PMID:16793551</ref>
==See Also==
 
*[[Pilin 3D structures|Pilin 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2co2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus cholerae-suis smith 1894]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ashcroft, A E]]
[[Category: Salmonella enterica]]
[[Category: Hannan, T J]]
[[Category: Ashcroft AE]]
[[Category: Hultgren, S J]]
[[Category: Hannan TJ]]
[[Category: Radford, S E]]
[[Category: Hultgren SJ]]
[[Category: Remaut, H]]
[[Category: Radford SE]]
[[Category: Rose, R J]]
[[Category: Remaut H]]
[[Category: Waksman, G]]
[[Category: Rose RJ]]
[[Category: Fibril protein]]
[[Category: Waksman G]]
[[Category: Fold complementation]]
[[Category: Pilus subunit]]

Latest revision as of 09:39, 1 May 2024

Salmonella enterica SafA pilin in complex with a 19-residue SafA Nte peptide (F3A mutant)Salmonella enterica SafA pilin in complex with a 19-residue SafA Nte peptide (F3A mutant)

Structural highlights

2co2 is a 2 chain structure with sequence from Salmonella enterica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8ZRK4_SALTY

See Also

2co2, resolution 2.30Å

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