5nqx: Difference between revisions
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==Structure of a fHbp(V1.1):PorA(P1.16) chimera. Fusion at fHbp position 294.== | ==Structure of a fHbp(V1.1):PorA(P1.16) chimera. Fusion at fHbp position 294.== | ||
<StructureSection load='5nqx' size='340' side='right' caption='[[5nqx]], [[Resolution|resolution]] 3.66Å' scene=''> | <StructureSection load='5nqx' size='340' side='right'caption='[[5nqx]], [[Resolution|resolution]] 3.66Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5nqx]] is a 5 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5nqx]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_MC58 Neisseria meningitidis MC58] and [https://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_C Neisseria meningitidis serogroup C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NQX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NQX 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]] 3.66Å</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=5nqx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nqx OCA], [https://pdbe.org/5nqx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nqx RCSB], [https://www.ebi.ac.uk/pdbsum/5nqx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nqx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/OMPA1_NEIMC OMPA1_NEIMC] Serves as a slightly cation selective porin. Major antigen on the gonococcal cell surface and it may have pathogenic properties in addition to its porin activity.[https://www.uniprot.org/uniprot/FHBP_NEIMB FHBP_NEIMB] A bacterial surface lipoprotein that binds host (human) complement factor H (fH, gene CFH), binding contributes to the avoidance of complement-mediated lysis by N.meningitidis. Binding of fH to the bacteria surface is independent of bacterial sialic acid moieties (PubMed:16751403). fH binding affinity is high enough that it may sequester plasma fH, depleting its circulating levels and de-regulating complement in the host (Probable). This protein induces high levels of bactericidal antibodies in mice (PubMed:12642606, PubMed:15039331, PubMed:15664958, PubMed:21753121, PubMed:23133374).<ref>PMID:12642606</ref> <ref>PMID:15039331</ref> <ref>PMID:15664958</ref> <ref>PMID:16751403</ref> <ref>PMID:21753121</ref> <ref>PMID:23133374</ref> <ref>PMID:19225461</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Neisseria meningitidis MC58]] | ||
[[Category: | [[Category: Neisseria meningitidis serogroup C]] | ||
[[Category: | [[Category: Johnson S]] | ||
[[Category: | [[Category: Jongerius I]] | ||
[[Category: | [[Category: Lea SM]] | ||
[[Category: | [[Category: Tang CM]] | ||