3d9x: Difference between revisions

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New page: '''Unreleased structure''' The entry 3d9x is ON HOLD Authors: Kornelius Zeth, Andrei Lupas, Joerg Martin Description: Structure of the head of the Bartonella adhesin BadA ''Page seed...
 
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'''Unreleased structure'''


The entry 3d9x is ON HOLD
==Structure of the head of the Bartonella adhesin BadA==
<StructureSection load='3d9x' size='340' side='right'caption='[[3d9x]], [[Resolution|resolution]] 1.13&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
</table>
== Function ==
[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d9/3d9x_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


Authors: Kornelius Zeth, Andrei Lupas, Joerg Martin
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>


Description: Structure of the head of the Bartonella adhesin BadA
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3d9x" style="background-color:#fffaf0;"></div>


 
==See Also==
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 09:38:32 2008''
*[[Adhesin 3D structures|Adhesin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bartonella henselae]]
[[Category: Large Structures]]
[[Category: Lupas A]]
[[Category: Martin J]]
[[Category: Zeth K]]

Latest revision as of 18:05, 1 November 2023

Structure of the head of the Bartonella adhesin BadAStructure of the head of the Bartonella adhesin BadA

Structural highlights

3d9x is a 3 chain structure with sequence from Bartonella henselae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.13Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).[1] [2] [3] [4] [5] [6]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Riess T, Andersson SG, Lupas A, Schaller M, Schäfer A, Kyme P, Martin J, Wälzlein JH, Ehehalt U, Lindroos H, Schirle M, Nordheim A, Autenrieth IB, Kempf VA. Bartonella adhesin a mediates a proangiogenic host cell response. J Exp Med. 2004 Nov 15;200(10):1267-78. PMID:15534369 doi:10.1084/jem.20040500
  2. ↑ Riess T, Raddatz G, Linke D, Schäfer A, Kempf VA. Analysis of Bartonella adhesin A expression reveals differences between various B. henselae strains. Infect Immun. 2007 Jan;75(1):35-43. PMID:17060468 doi:10.1128/IAI.00963-06
  3. ↑ Kaiser PO, Riess T, Wagner CL, Linke D, Lupas AN, Schwarz H, Raddatz G, Schäfer A, Kempf VA. The head of Bartonella adhesin A is crucial for host cell interaction of Bartonella henselae. Cell Microbiol. 2008 Nov;10(11):2223-34. PMID:18627378 doi:10.1111/j.1462-5822.2008.01201.x
  4. ↑ Müller NF, Kaiser PO, Linke D, Schwarz H, Riess T, Schäfer A, Eble JA, Kempf VA. Trimeric autotransporter adhesin-dependent adherence of Bartonella henselae, Bartonella quintana, and Yersinia enterocolitica to matrix components and endothelial cells under static and dynamic flow conditions. Infect Immun. 2011 Jul;79(7):2544-53. PMID:21536788 doi:10.1128/IAI.01309-10
  5. ↑ Lu YY, Franz B, Truttmann MC, Riess T, Gay-Fraret J, Faustmann M, Kempf VA, Dehio C. Bartonella henselae trimeric autotransporter adhesin BadA expression interferes with effector translocation by the VirB/D4 type IV secretion system. Cell Microbiol. 2013 May;15(5):759-78. PMID:23163798 doi:10.1111/cmi.12070
  6. ↑ Lu YY, Franz B, Truttmann MC, Riess T, Gay-Fraret J, Faustmann M, Kempf VA, Dehio C. Bartonella henselae trimeric autotransporter adhesin BadA expression interferes with effector translocation by the VirB/D4 type IV secretion system. Cell Microbiol. 2013 May;15(5):759-78. PMID:23163798 doi:10.1111/cmi.12070
  7. ↑ Szczesny P, Linke D, Ursinus A, Bar K, Schwarz H, Riess TM, Kempf VA, Lupas AN, Martin J, Zeth K. Structure of the head of the Bartonella adhesin BadA. PLoS Pathog. 2008 Aug 8;4(8):e1000119. PMID:18688279 doi:10.1371/journal.ppat.1000119

3d9x, resolution 1.13Å

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