3jwn

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{{Seed}}
 
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[[Image:3jwn.jpg|left|200px]]
 
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==Complex of FimC, FimF, FimG and FimH==
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The line below this paragraph, containing "STRUCTURE_3jwn", creates the "Structure Box" on the page.
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<StructureSection load='3jwn' size='340' side='right'caption='[[3jwn]], [[Resolution|resolution]] 2.69&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'>[[3jwn]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_F18+ Escherichia coli F18+] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JWN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JWN 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]] 2.69&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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{{STRUCTURE_3jwn| PDB=3jwn | SCENE= }}
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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=3jwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jwn OCA], [https://pdbe.org/3jwn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jwn RCSB], [https://www.ebi.ac.uk/pdbsum/3jwn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jwn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FIMG_ECOLI FIMG_ECOLI] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Involved in the integration of FimH in the fimbriae.
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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/jw/3jwn_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=3jwn 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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The Escherichia coli fimbrial adhesive protein, FimH, mediates shear-dependent binding to mannosylated surfaces via force-enhanced allosteric catch bonds, but the underlying structural mechanism was previously unknown. Here we present the crystal structure of FimH incorporated into the multiprotein fimbrial tip, where the anchoring (pilin) domain of FimH interacts with the mannose-binding (lectin) domain and causes a twist in the beta sandwich fold of the latter. This loosens the mannose-binding pocket on the opposite end of the lectin domain, resulting in an inactive low-affinity state of the adhesin. The autoinhibition effect of the pilin domain is removed by application of tensile force across the bond, which separates the domains and causes the lectin domain to untwist and clamp tightly around the ligand like a finger-trap toy. Thus, beta sandwich domains, which are common in multidomain proteins exposed to tensile force in vivo, can undergo drastic allosteric changes and be subjected to mechanical regulation.
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===Complex of FimC, FimF, FimG and FimH===
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Structural basis for mechanical force regulation of the adhesin FimH via finger trap-like beta sheet twisting.,Le Trong I, Aprikian P, Kidd BA, Forero-Shelton M, Tchesnokova V, Rajagopal P, Rodriguez V, Interlandi G, Klevit R, Vogel V, Stenkamp RE, Sokurenko EV, Thomas WE Cell. 2010 May 14;141(4):645-55. PMID:20478255<ref>PMID:20478255</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_20478255}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3jwn" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20478255 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20478255}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia coli F18+]]
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3JWN is a 10 chains structure with 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=3JWN OCA].
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[[Category: Escherichia coli K-12]]
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[[Category: Large Structures]]
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==Reference==
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[[Category: Aprikian P]]
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<ref group="xtra">PMID:20478255</ref><references group="xtra"/>
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[[Category: Le Trong I]]
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[[Category: Escherichia coli]]
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[[Category: Sokurenko EV]]
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[[Category: Aprikian, P.]]
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[[Category: Stenkamp RE]]
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[[Category: Sokurenko, E V.]]
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[[Category: Stenkamp, R E.]]
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[[Category: Trong, I Le.]]
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[[Category: Cell adhesion]]
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[[Category: Chaperone]]
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[[Category: Disulfide bond]]
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[[Category: Fibrium]]
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[[Category: Fimbria]]
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[[Category: Fimbrium]]
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[[Category: Fimc]]
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[[Category: Fimf]]
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[[Category: Fimg]]
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[[Category: Fimh]]
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[[Category: Immunoglobulin domain]]
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[[Category: Periplasm]]
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[[Category: Protein binding-cell adhesion complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 16 08:38:22 2010''
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Current revision

Complex of FimC, FimF, FimG and FimH

PDB ID 3jwn

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