1z2y: Difference between revisions
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[[ | ==THEORETICAL MODEL OF MENINGOCOCCAL TRANSFERRIN-BINDING PROTEIN A== | ||
<StructureSection load='1z2y' size='340' side='right'caption='[[1z2y]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z2Y FirstGlance]. <br> | |||
</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=1z2y FirstGlance], [https://www.ebi.ac.uk/pdbsum/1z2y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z2y ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Neisseria meningitidis, a causative agent of bacterial meningitis, obtains transferrin-bound iron by expressing two outer membrane located transferrin-binding proteins, TbpA and TbpB. TbpA is thought to be an integral outer membrane pore that facilitates iron uptake. Evidence suggests that TbpA is a useful antigen for inclusion in a vaccine effective against meningococcal disease, hence the identification of regions involved in ligand binding is of paramount importance to design strategies to block uptake of iron. The protein shares sequence and functional similarities to the Escherichia coli siderophore receptors FepA and FhuA, whose structures have been determined. These receptors are composed of two domains, a 22-stranded beta-barrel and an N-terminal plug region that sits within the barrel and occludes the transmembrane pore. A three-dimensional TbpA model was constructed using FepA and FhuA structural templates, hydrophobicity analysis and homology modelling. TbpA was found to possess a similar architecture to the siderophore receptors. In addition to providing insights into the highly immunogenic nature of TbpA and allowing the prediction of potentially important ligand-binding epitopes, the model also reveals a narrow channel through its entire length. The relevance of this channel and the spatial arrangement of external loops, to the mechanism of iron translocation employed by TbpA is discussed. | |||
Homology modelling of transferrin-binding protein A from Neisseria meningitidis.,Oakhill JS, Sutton BJ, Gorringe AR, Evans RW Protein Eng Des Sel. 2005 May;18(5):221-8. Epub 2005 Apr 8. PMID:15820975<ref>PMID:15820975</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 1z2y" style="background-color:#fffaf0;"></div> | |||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Evans, R W]] | [[Category: Evans, R W]] | ||
[[Category: Gorringe, A R]] | [[Category: Gorringe, A R]] | ||
[[Category: Oakhill, J S]] | [[Category: Oakhill, J S]] | ||
[[Category: Sutton, B J]] | [[Category: Sutton, B J]] | ||
Latest revision as of 19:36, 3 November 2021
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THEORETICAL MODEL OF MENINGOCOCCAL TRANSFERRIN-BINDING PROTEIN ATHEORETICAL MODEL OF MENINGOCOCCAL TRANSFERRIN-BINDING PROTEIN A
Structural highlights
Publication Abstract from PubMedNeisseria meningitidis, a causative agent of bacterial meningitis, obtains transferrin-bound iron by expressing two outer membrane located transferrin-binding proteins, TbpA and TbpB. TbpA is thought to be an integral outer membrane pore that facilitates iron uptake. Evidence suggests that TbpA is a useful antigen for inclusion in a vaccine effective against meningococcal disease, hence the identification of regions involved in ligand binding is of paramount importance to design strategies to block uptake of iron. The protein shares sequence and functional similarities to the Escherichia coli siderophore receptors FepA and FhuA, whose structures have been determined. These receptors are composed of two domains, a 22-stranded beta-barrel and an N-terminal plug region that sits within the barrel and occludes the transmembrane pore. A three-dimensional TbpA model was constructed using FepA and FhuA structural templates, hydrophobicity analysis and homology modelling. TbpA was found to possess a similar architecture to the siderophore receptors. In addition to providing insights into the highly immunogenic nature of TbpA and allowing the prediction of potentially important ligand-binding epitopes, the model also reveals a narrow channel through its entire length. The relevance of this channel and the spatial arrangement of external loops, to the mechanism of iron translocation employed by TbpA is discussed. Homology modelling of transferrin-binding protein A from Neisseria meningitidis.,Oakhill JS, Sutton BJ, Gorringe AR, Evans RW Protein Eng Des Sel. 2005 May;18(5):221-8. Epub 2005 Apr 8. PMID:15820975[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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