View source for 3hoe


==Crystal Structure of Surface Lipoprotein==
<StructureSection load='3hoe' size='340' side='right' caption='[[3hoe]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3hoe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Actpl Actpl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HOE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HOE FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hol|3hol]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tbpB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=715 ACTPL])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3hoe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hoe OCA], [http://pdbe.org/3hoe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hoe RCSB], [http://www.ebi.ac.uk/pdbsum/3hoe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hoe ProSAT]</span></td></tr>
</table>
== 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/ho/3hoe_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=3hoe ConSurf].
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== Publication Abstract from PubMed ==
Pathogenic bacteria from the Neisseriaceae and Pasteurellacea families acquire iron directly from the host iron-binding glycoprotein, transferrin (Tf), in a process mediated by surface receptor proteins that directly bind host Tf, extract the iron, and transport it across the outer membrane. The bacterial Tf receptor is comprised of a surface exposed lipoprotein, Tf-binding protein B (TbpB), and an integral outer-membrane protein, Tf-binding protein A (TbpA), both of which are essential for survival in the host. In this study, we report the 1.98 A resolution structure of TbpB from the porcine pathogen Actinobacillus pleuropneumoniae, providing insights into the mechanism of Tf binding and the role of TbpB. A model for the complex of TbpB bound to Tf is proposed. Mutation of a single surface-exposed Phe residue on TbpB within the predicted interface completely abolishes binding to Tf, suggesting that the TbpB N lobe comprises the sole high-affinity binding region for Tf.

Insights into the bacterial transferrin receptor: the structure of transferrin-binding protein B from Actinobacillus pleuropneumoniae.,Moraes TF, Yu RH, Strynadka NC, Schryvers AB Mol Cell. 2009 Aug 28;35(4):523-33. PMID:19716795<ref>PMID:19716795</ref>

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

==See Also==
*[[Transferrin-binding protein|Transferrin-binding protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Actpl]]
[[Category: Moraes, T F]]
[[Category: Schryvers, A B]]
[[Category: Strynadka, N C.J]]
[[Category: Yu, R H]]
[[Category: Ion transport]]
[[Category: Iron acquisition]]
[[Category: Receptor]]
[[Category: Transferrin]]
[[Category: Transport protein]]
[[Category: Vaccine]]