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<StructureSection load='3hoe' size='340' side='right'caption='[[3hoe]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3hoe' size='340' side='right'caption='[[3hoe]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3hoe]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3HOE FirstGlance]. <br>
<table><tr><td colspan='2'>[[3hoe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinobacillus_pleuropneumoniae Actinobacillus pleuropneumoniae]. 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 [https://proteopedia.org/fgij/fg.htm?mol=3HOE FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3hol|3hol]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.303&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tbpB ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3hoe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hoe OCA], [https://pdbe.org/3hoe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hoe RCSB], [https://www.ebi.ac.uk/pdbsum/3hoe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hoe ProSAT]</span></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=3hoe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hoe OCA], [https://pdbe.org/3hoe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hoe RCSB], [https://www.ebi.ac.uk/pdbsum/3hoe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hoe ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q44124_ACTPL Q44124_ACTPL]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=3hoe ConSurf].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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>
</div>
<div class="pdbe-citations 3hoe" style="background-color:#fffaf0;"></div>


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

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