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| | ==Crystal structure of the Neisseria meningitidis iron-regulated outer membrane lipoprotein FrpD== | | ==Crystal structure of the Neisseria meningitidis iron-regulated outer membrane lipoprotein FrpD== |
| - | <StructureSection load='5edj' size='340' side='right' caption='[[5edj]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='5edj' size='340' side='right'caption='[[5edj]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5edj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Neimb Neimb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EDJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EDJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5edj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_MC58 Neisseria meningitidis MC58]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EDJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EDJ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5edf|5edf]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LA50_03295 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=122586 NEIMB])</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=5edj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5edj OCA], [https://pdbe.org/5edj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5edj RCSB], [https://www.ebi.ac.uk/pdbsum/5edj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5edj ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5edj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5edj OCA], [http://pdbe.org/5edj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5edj RCSB], [http://www.ebi.ac.uk/pdbsum/5edj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5edj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9K129_NEIMB Q9K129_NEIMB] |
| | <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: Neimb]] | + | [[Category: Large Structures]] |
| - | [[Category: Bumba, L]] | + | [[Category: Neisseria meningitidis MC58]] |
| - | [[Category: Rezacova, P]] | + | [[Category: Bumba L]] |
| - | [[Category: Sebo, P]]
| + | [[Category: Kuta Smatanova I]] |
| - | [[Category: Smatanova, I Kuta]] | + | [[Category: Rezacova P]] |
| - | [[Category: Sviridova, E]] | + | [[Category: Sebo P]] |
| - | [[Category: Frpc-binding protein]] | + | [[Category: Sviridova E]] |
| - | [[Category: Iron-regulated protein frpd]] | + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Novel fold]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
Q9K129_NEIMB
Publication Abstract from PubMed
The iron-regulated protein FrpD from Neisseria meningitidis is an outer membrane lipoprotein that interacts with very high affinity (Kd ~ 0.2 nM) with the N-terminal domain of FrpC, a Type I-secreted protein from the Repeat in ToXin (RTX) protein family. In the presence of Ca2+, FrpC undergoes Ca2+ -dependent protein trans-splicing that includes an autocatalytic cleavage of the Asp414-Pro415 peptide bond and formation of an Asp414-Lys isopeptide bond. Here, we report the high-resolution structure of FrpD and describe the structure-function relationships underlying the interaction between FrpD and FrpC1-414. We identified FrpD residues involved in FrpC1-414 binding, which enabled localization of FrpD within the low-resolution SAXS model of the FrpD-FrpC1-414 complex. Moreover, the trans-splicing activity of FrpC resulted in covalent linkage of the FrpC1-414 fragment to plasma membrane proteins of epithelial cells in vitro, suggesting that formation of the FrpD-FrpC1-414 complex may be involved in the interaction of meningococci with the host cell surface.
Structural basis of the interaction between the putative adhesion-involved and iron-regulated FrpD and FrpC proteins of Neisseria meningitidis.,Sviridova E, Rezacova P, Bondar A, Veverka V, Novak P, Schenk G, Svergun DI, Kuta Smatanova I, Bumba L Sci Rep. 2017 Jan 13;7:40408. doi: 10.1038/srep40408. PMID:28084396[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sviridova E, Rezacova P, Bondar A, Veverka V, Novak P, Schenk G, Svergun DI, Kuta Smatanova I, Bumba L. Structural basis of the interaction between the putative adhesion-involved and iron-regulated FrpD and FrpC proteins of Neisseria meningitidis. Sci Rep. 2017 Jan 13;7:40408. doi: 10.1038/srep40408. PMID:28084396 doi:http://dx.doi.org/10.1038/srep40408
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