3hoe
From Proteopedia
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<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 [https://en.wikipedia.org/wiki/ | + | <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=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.303Å</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=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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, 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: | + | [[Category: Actinobacillus pleuropneumoniae]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Moraes | + | [[Category: Moraes TF]] |
| - | [[Category: Schryvers | + | [[Category: Schryvers AB]] |
| - | [[Category: Strynadka | + | [[Category: Strynadka NCJ]] |
| - | [[Category: Yu | + | [[Category: Yu RH]] |
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Current revision
Crystal Structure of Surface Lipoprotein
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