3pr7

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Current revision (10:42, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3pr7' size='340' side='right'caption='[[3pr7]], [[Resolution|resolution]] 2.94&Aring;' scene=''>
<StructureSection load='3pr7' size='340' side='right'caption='[[3pr7]], [[Resolution|resolution]] 2.94&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3pr7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"mikrokkokus_catarrhalis"_(sic)_frosch_and_kolle_in_flugge_1896 "mikrokkokus catarrhalis" (sic) frosch and kolle in flugge 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PR7 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3pr7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Moraxella_catarrhalis Moraxella catarrhalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PR7 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ntn|3ntn]]</div></td></tr>
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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]] 2.94&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uspA1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=480 "Mikrokkokus catarrhalis" (sic) Frosch and Kolle in Flugge 1896])</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=3pr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pr7 OCA], [https://pdbe.org/3pr7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pr7 RCSB], [https://www.ebi.ac.uk/pdbsum/3pr7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pr7 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=3pr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pr7 OCA], [https://pdbe.org/3pr7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pr7 RCSB], [https://www.ebi.ac.uk/pdbsum/3pr7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pr7 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q9XD56_MORCA Q9XD56_MORCA]
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Bacterial cell surfaces are commonly decorated with a layer formed from multiple copies of adhesin proteins whose binding interactions initiate colonization and infection processes. In this study, we investigate the physical deformability of the UspA1 adhesin protein from Moraxella catarrhalis, a causative agent of middle-ear infections in humans. UspA1 binds a range of extracellular proteins including fibronectin, and the epithelial cellular receptor carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1). Electron microscopy indicates that unliganded UspA1 is densely packed at, and extends about 800 A from, the Moraxella surface. Using a modified atomic force microscope, we show that the adhesive properties and thickness of the UspA1 layer at the cell surface varies on addition of either fibronectin or CEACAM1. This in situ analysis is then correlated with the molecular structure of UspA1. To provide an overall model for UspA1, we have determined crystal structures for two N-terminal fragments which are then combined with a previous structure of the CEACAM1-binding site. We show that the UspA1-fibronectin complex is formed between UspA1 head region and the 13th type-III domain of fibronectin and, using X-ray scattering, that the complex involves an angular association between these two proteins. In combination with a previous study, which showed that the CEACAM1-UspA1 complex is distinctively bent in solution, we correlate these observations on isolated fragments of UspA1 with its in situ response on the cell surface. This study therefore provides a rare direct demonstration of protein conformational change at the cell surface.
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Correlation of in situ mechanosensitive responses of the Moraxella catarrhalis adhesin UspA1 with fibronectin and receptor CEACAM1 binding.,Agnew C, Borodina E, Zaccai NR, Conners R, Burton NM, Vicary JA, Cole DK, Antognozzi M, Virji M, Brady RL Proc Natl Acad Sci U S A. 2011 Aug 29. PMID:21876142<ref>PMID:21876142</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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<div class="pdbe-citations 3pr7" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Agnew, C R.J]]
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[[Category: Moraxella catarrhalis]]
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[[Category: Brady, R L]]
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[[Category: Agnew CRJ]]
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[[Category: Conners, R]]
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[[Category: Brady RL]]
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[[Category: Zaccai, N R]]
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[[Category: Conners R]]
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[[Category: Adhesin]]
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[[Category: Zaccai NR]]
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[[Category: Beta-roll and coiled-coil]]
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[[Category: Extracellular]]
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[[Category: Membrane protein]]
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Current revision

Multi-functional and mechanosensitive receptor binding activity of the Moraxella catarrhalis adhesin UspA1

PDB ID 3pr7

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