3hoe: Difference between revisions
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==Crystal Structure of Surface Lipoprotein== | ==Crystal Structure of Surface Lipoprotein== | ||
<StructureSection load='3hoe' size='340' side='right' caption='[[3hoe]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='3hoe' size='340' side='right'caption='[[3hoe]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3hoe]] is a 2 chain structure with sequence from [ | <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> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hol|3hol]]</td></tr> | </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> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tbpB ([ | <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'>[ | <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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Actpl]] | [[Category: Actpl]] | ||
[[Category: Large Structures]] | |||
[[Category: Moraes, T F]] | [[Category: Moraes, T F]] | ||
[[Category: Schryvers, A B]] | [[Category: Schryvers, A B]] | ||
Revision as of 15:54, 23 March 2022
Crystal Structure of Surface LipoproteinCrystal Structure of Surface Lipoprotein
Structural highlights
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 PubMedPathogenic 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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