5EDJ
Crystal structure of the Neisseria meningitidis iron-regulated outer membrane lipoprotein FrpD
Summary for 5EDJ
| Entry DOI | 10.2210/pdb5edj/pdb |
| Related | 5EDF |
| Descriptor | FrpC operon protein (2 entities in total) |
| Functional Keywords | iron-regulated protein frpd, frpc-binding protein, novel fold, membrane protein, unknown function |
| Biological source | Neisseria meningitidis MC58 |
| Total number of polymer chains | 1 |
| Total formula weight | 27027.99 |
| Authors | Sviridova, E.,Bumba, L.,Rezacova, P.,Sebo, P.,Kuta Smatanova, I. (deposition date: 2015-10-21, release date: 2017-02-01, Last modification date: 2024-01-10) |
| Primary citation | Sviridova, E.,Rezacova, P.,Bondar, A.,Veverka, V.,Novak, P.,Schenk, G.,Svergun, D.I.,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, 7:40408-40408, 2017 Cited by PubMed Abstract: The iron-regulated protein FrpD from Neisseria meningitidis is an outer membrane lipoprotein that interacts with very high affinity (K ~ 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 Ca, FrpC undergoes Ca -dependent protein trans-splicing that includes an autocatalytic cleavage of the Asp-Pro peptide bond and formation of an Asp-Lys isopeptide bond. Here, we report the high-resolution structure of FrpD and describe the structure-function relationships underlying the interaction between FrpD and FrpC. We identified FrpD residues involved in FrpC binding, which enabled localization of FrpD within the low-resolution SAXS model of the FrpD-FrpC complex. Moreover, the trans-splicing activity of FrpC resulted in covalent linkage of the FrpC fragment to plasma membrane proteins of epithelial cells in vitro, suggesting that formation of the FrpD-FrpC complex may be involved in the interaction of meningococci with the host cell surface. PubMed: 28084396DOI: 10.1038/srep40408 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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