2bcm

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{{Seed}}
 
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[[Image:2bcm.png|left|200px]]
 
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==DaaE adhesin==
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The line below this paragraph, containing "STRUCTURE_2bcm", creates the "Structure Box" on the page.
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<StructureSection load='2bcm' size='340' side='right'caption='[[2bcm]], [[Resolution|resolution]] 1.48&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'>[[2bcm]] is a 3 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=2BCM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BCM 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]] 1.48&#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=2bcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bcm OCA], [https://pdbe.org/2bcm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bcm RCSB], [https://www.ebi.ac.uk/pdbsum/2bcm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bcm ProSAT]</span></td></tr>
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{{STRUCTURE_2bcm| PDB=2bcm | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DAAE_ECOLX DAAE_ECOLX] Hemagglutinins of uropathogenic E.coli mediate adherence to the upper urinary tract. These adhesins bind to the Dr blood group antigen and also agglutinate human erythrocytes in the presence of D-mannose (mannose-resistant hemagglutination (MRHA)). C1845 is a strain responsible for diarrheal disease.
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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/bc/2bcm_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=2bcm 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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DaaE is a member of the Dr adhesin family of Escherichia coli, members of which are associated with diarrhea and urinary tract infections. A receptor for Dr adhesins is the cell surface protein, decay-accelerating factor (DAF). We have carried out a functional analysis of Dr adhesins, as well as mutagenesis and crystallographic studies of DaaE, to obtain detailed molecular information about interactions of Dr adhesins with their receptors. The crystal structure of DaaE has been solved at 1.48 A resolution. Trimers of the protein are found in the crystal, as has been the case for other Dr adhesins. Naturally occurring variants and directed mutations in DaaE have been generated and analyzed for their ability to bind DAF. Mapping of the mutation sites onto the DaaE molecular structure shows that several of them contribute to a contiguous surface that is likely the primary DAF-binding site. The DAF-binding properties of purified fimbriae and adhesin proteins from mutants and variants correlated with the ability of bacteria expressing these proteins to bind to human epithelial cells in culture. DaaE, DraE, AfaE-III, and AfaE-V interact with complement control protein (CCP) domains 2-4 of DAF, and analysis of the ionic strength dependence of their binding indicates that the intermolecular interactions are highly electrostatic in nature. The adhesins AfaE-I and NfaE-2 bind to CCP-3 and CCP-4 of DAF, and electrostatic interactions contribute significantly less to these interactions. These observations are consistent with structural predictions for these Dr variants and also suggest a role for the positively charged region linking CCP-2 and CCP-3 of DAF in electrostatic Dr adhesin-DAF interactions.
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===DaaE adhesin===
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Crystal structure and mutational analysis of the DaaE adhesin of Escherichia coli.,Korotkova N, Le Trong I, Samudrala R, Korotkov K, Van Loy CP, Bui AL, Moseley SL, Stenkamp RE J Biol Chem. 2006 Aug 4;281(31):22367-77. Epub 2006 Jun 2. PMID:16751628<ref>PMID:16751628</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_16751628}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2bcm" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16751628 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16751628}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2BCM is a 3 chains structure of 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=2BCM OCA].
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==Reference==
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<ref group="xtra">PMID:16751628</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Korotkova, N.]]
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[[Category: Large Structures]]
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[[Category: Moseley, S.]]
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[[Category: Korotkova N]]
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[[Category: Stenkamp, R E.]]
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[[Category: Le Trong I]]
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[[Category: Trong, I Le.]]
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[[Category: Moseley S]]
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[[Category: Daae adhesin]]
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[[Category: Stenkamp RE]]
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[[Category: Donor strand complementation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 01:08:54 2009''
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Current revision

DaaE adhesin

PDB ID 2bcm

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