3d9x

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{{Seed}}
 
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[[Image:3d9x.jpg|left|200px]]
 
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==Structure of the head of the Bartonella adhesin BadA==
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The line below this paragraph, containing "STRUCTURE_3d9x", creates the "Structure Box" on the page.
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<StructureSection load='3d9x' size='340' side='right'caption='[[3d9x]], [[Resolution|resolution]] 1.13&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'>[[3d9x]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bartonella_henselae Bartonella henselae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D9X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D9X 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]] 1.13&#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=3d9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d9x OCA], [https://pdbe.org/3d9x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d9x RCSB], [https://www.ebi.ac.uk/pdbsum/3d9x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d9x ProSAT]</span></td></tr>
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{{STRUCTURE_3d9x| PDB=3d9x | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BADA_BARHN BADA_BARHN] Mediates bacterial adherence to host endothelial cells and host extracellular matrix proteins (collagen type I, III, IV, laminin and fibronectin). Static versus dynamic adherence results differ slightly; in dynamic adherence studies bacteria bind to fixed components under a constant defined flow rate to simulate in vivo infection conditions (PubMed:15534369, PubMed:17060468, PubMed:18627378, PubMed:21536788, PubMed:23163798). Induces secretion of host proangiogenic cytokines such as VEGFA, ADM, IGFBP-3 and IL-8. May prevent bacterial phagocytosis by macrophages (PubMed:15534369) (Probable). Probably mediates bacterial autoagglutination (PubMed:17060468, PubMed:18627378). Negatively impacts type IV secretion system effectors (VirB/D4 T4SS and its substrate Bep proteins), possibly by preventing close association of host and bacterial cells. This implies the 2 factors are expressed at different times during infection (Probable).<ref>PMID:15534369</ref> <ref>PMID:17060468</ref> <ref>PMID:18627378</ref> <ref>PMID:21536788</ref> <ref>PMID:23163798</ref> <ref>PMID:23163798</ref>
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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/d9/3d9x_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3d9x 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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Trimeric autotransporter adhesins (TAAs) are a major class of proteins by which pathogenic proteobacteria adhere to their hosts. Prominent examples include Yersinia YadA, Haemophilus Hia and Hsf, Moraxella UspA1 and A2, and Neisseria NadA. TAAs also occur in symbiotic and environmental species and presumably represent a general solution to the problem of adhesion in proteobacteria. The general structure of TAAs follows a head-stalk-anchor architecture, where the heads are the primary mediators of attachment and autoagglutination. In the major adhesin of Bartonella henselae, BadA, the head consists of three domains, the N-terminal of which shows strong sequence similarity to the head of Yersinia YadA. The two other domains were not recognizably similar to any protein of known structure. We therefore determined their crystal structure to a resolution of 1.1 A. Both domains are beta-prisms, the N-terminal one formed by interleaved, five-stranded beta-meanders parallel to the trimer axis and the C-terminal one by five-stranded beta-meanders orthogonal to the axis. Despite the absence of statistically significant sequence similarity, the two domains are structurally similar to domains from Haemophilus Hia, albeit in permuted order. Thus, the BadA head appears to be a chimera of domains seen in two other TAAs, YadA and Hia, highlighting the combinatorial evolutionary strategy taken by pathogens.
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===Structure of the head of the Bartonella adhesin BadA===
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Structure of the head of the Bartonella adhesin BadA.,Szczesny P, Linke D, Ursinus A, Bar K, Schwarz H, Riess TM, Kempf VA, Lupas AN, Martin J, Zeth K PLoS Pathog. 2008 Aug 8;4(8):e1000119. PMID:18688279<ref>PMID:18688279</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 3d9x" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18688279}}, adds the Publication Abstract to the page
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*[[Adhesin 3D structures|Adhesin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18688279 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18688279}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3D9X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bartonella_henselae Bartonella henselae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D9X OCA].
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==Reference==
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Structure of the head of the Bartonella adhesin BadA., Szczesny P, Linke D, Ursinus A, Bar K, Schwarz H, Riess TM, Kempf VA, Lupas AN, Martin J, Zeth K, PLoS Pathog. 2008 Aug 8;4(8):e1000119. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18688279 18688279]
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[[Category: Bartonella henselae]]
[[Category: Bartonella henselae]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Lupas, A.]]
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[[Category: Lupas A]]
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[[Category: Martin, J.]]
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[[Category: Martin J]]
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[[Category: Zeth, K.]]
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[[Category: Zeth K]]
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[[Category: Bada]]
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[[Category: Cell adhesion]]
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[[Category: High resolution]]
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[[Category: Structure module]]
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[[Category: Trimeric adhesin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 27 11:30:00 2008''
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Current revision

Structure of the head of the Bartonella adhesin BadA

PDB ID 3d9x

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