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2pyb
From Proteopedia
(Difference between revisions)
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<StructureSection load='2pyb' size='340' side='right'caption='[[2pyb]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='2pyb' size='340' side='right'caption='[[2pyb]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2pyb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2pyb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Borreliella_burgdorferi_B31 Borreliella burgdorferi B31]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PYB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PYB 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]] 2.6Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></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=2pyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pyb OCA], [https://pdbe.org/2pyb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pyb RCSB], [https://www.ebi.ac.uk/pdbsum/2pyb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pyb 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=2pyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pyb OCA], [https://pdbe.org/2pyb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pyb RCSB], [https://www.ebi.ac.uk/pdbsum/2pyb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pyb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/O51633_BORBU O51633_BORBU] | ||
== 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=2pyb 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=2pyb ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | NapA from Borrelia burgdorferi is a member of the Dps-like protein family with specific immunomodulatory properties; in particular, NapA is able to induce the expression of IL-23 in neutrophils and monocytes, as well as the expression of IL-6, IL-1beta, and transforming growth factor beta (TGF-beta) in monocytes, via Toll-like receptor (TLR) 2. Such an activity on innate immune cells triggers a synovial fluid Th17 response. Here we report the crystal structure of NapA, determined at 2.6A resolution, which shows that the quaternary structure of the protein is that of a dodecamer with 23 symmetry, typical of the proteins of the family. We also demonstrate that the N- and C-terminal tails, which are flexible and not visible in the crystal, are not relevant for its pro-Th17 activity. Based on the crystal structure and on the comparison with the structure of the orthologous protein from Helicobacter pylori, HP-NAP, we hypothesize that the charge distributions on the two proteins' surfaces are responsible for the interaction with TLR2 and for the different behaviors in modulating the immune response. | ||
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| - | Structure and immunomodulatory property relationship in NapA of Borrelia burgdorferi.,Codolo G, Papinutto E, Polenghi A, D'Elios MM, Zanotti G, de Bernard M Biochim Biophys Acta. 2010 Dec;1804(12):2191-7. doi:, 10.1016/j.bbapap.2010.09.004. Epub 2010 Sep 19. PMID:20851780<ref>PMID:20851780</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2pyb" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Borreliella burgdorferi B31]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Bernard | + | [[Category: De Bernard M]] |
| - | [[Category: Papinutto | + | [[Category: Papinutto E]] |
| - | [[Category: Zanotti | + | [[Category: Zanotti G]] |
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Current revision
Napa protein from borrelia burgdorferi
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