2m4f: Difference between revisions
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==Solution Structure of Outer surface protein E== | |||
<StructureSection load='2m4f' size='340' side='right'caption='[[2m4f]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2m4f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Borreliella_burgdorferi_N40 Borreliella burgdorferi N40]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M4F FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2m4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m4f OCA], [https://pdbe.org/2m4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m4f RCSB], [https://www.ebi.ac.uk/pdbsum/2m4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m4f ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Borrelia burgdorferi spirochetes that cause Lyme borreliosis survive for a long time in human serum because they successfully evade the complement system, an important arm of innate immunity. The outer surface protein E (OspE) of B. burgdorferi is needed for this because it recruits complement regulator factor H (FH) onto the bacterial surface to evade complement-mediated cell lysis. To understand this process at the molecular level, we used a structural approach. First, we solved the solution structure of OspE by NMR, revealing a fold that has not been seen before in proteins involved in complement regulation. Next, we solved the x-ray structure of the complex between OspE and the FH C-terminal domains 19 and 20 (FH19-20) at 2.83 A resolution. The structure shows that OspE binds FH19-20 in a way similar to, but not identical with, that used by endothelial cells to bind FH via glycosaminoglycans. The observed interaction of OspE with FH19-20 allows the full function of FH in down-regulation of complement activation on the bacteria. This reveals the molecular basis for how B. burgdorferi evades innate immunity and suggests how OspE could be used as a potential vaccine antigen. | |||
Structural Basis for Complement Evasion by Lyme Disease Pathogen Borrelia burgdorferi.,Bhattacharjee A, Oeemig JS, Kolodziejczyk R, Meri T, Kajander T, Lehtinen MJ, Iwai H, Jokiranta TS, Goldman A J Biol Chem. 2013 Jun 28;288(26):18685-95. doi: 10.1074/jbc.M113.459040. Epub, 2013 May 8. PMID:23658013<ref>PMID:23658013</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2m4f" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Outer surface protein|Outer surface protein]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Borreliella burgdorferi N40]] | |||
[[Category: Large Structures]] | |||
[[Category: Bhattacharjee A]] | |||
[[Category: Goldman A]] | |||
[[Category: Iwai H]] | |||
[[Category: Jokiranta T]] | |||
[[Category: Kajander T]] | |||
[[Category: Kolodziejczyk R]] | |||
[[Category: Meri T]] | |||
[[Category: Oeemig JS]] | |||
Latest revision as of 08:59, 15 May 2024
Solution Structure of Outer surface protein ESolution Structure of Outer surface protein E
Structural highlights
Publication Abstract from PubMedBorrelia burgdorferi spirochetes that cause Lyme borreliosis survive for a long time in human serum because they successfully evade the complement system, an important arm of innate immunity. The outer surface protein E (OspE) of B. burgdorferi is needed for this because it recruits complement regulator factor H (FH) onto the bacterial surface to evade complement-mediated cell lysis. To understand this process at the molecular level, we used a structural approach. First, we solved the solution structure of OspE by NMR, revealing a fold that has not been seen before in proteins involved in complement regulation. Next, we solved the x-ray structure of the complex between OspE and the FH C-terminal domains 19 and 20 (FH19-20) at 2.83 A resolution. The structure shows that OspE binds FH19-20 in a way similar to, but not identical with, that used by endothelial cells to bind FH via glycosaminoglycans. The observed interaction of OspE with FH19-20 allows the full function of FH in down-regulation of complement activation on the bacteria. This reveals the molecular basis for how B. burgdorferi evades innate immunity and suggests how OspE could be used as a potential vaccine antigen. Structural Basis for Complement Evasion by Lyme Disease Pathogen Borrelia burgdorferi.,Bhattacharjee A, Oeemig JS, Kolodziejczyk R, Meri T, Kajander T, Lehtinen MJ, Iwai H, Jokiranta TS, Goldman A J Biol Chem. 2013 Jun 28;288(26):18685-95. doi: 10.1074/jbc.M113.459040. Epub, 2013 May 8. PMID:23658013[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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