English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Tools annual

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Presents the access of premium content as premium feature

Premium Content

Global: Zendy Plus annual

Global: Zendy Free Plan

The iron-regulated protein FrpD from  Neisseria meningitidis  is an outer membrane lipoprotein that interacts with very high affinity ( K   d   ~ 0.2 nM) with the N-terminal domain of FrpC, a Type I-secreted protein from the  R epeat in  T o X in (RTX) protein family. In the presence of Ca 2+ , FrpC undergoes Ca 2+  -dependent protein  trans -splicing that includes an autocatalytic cleavage of the Asp 414 -Pro 415  peptide bond and formation of an Asp 414 -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 1-414 . We identified FrpD residues involved in FrpC 1-414  binding, which enabled localization of FrpD within the low-resolution SAXS model of the FrpD-FrpC 1-414  complex. Moreover, the  trans -splicing activity of FrpC resulted in covalent linkage of the FrpC 1-414  fragment to plasma membrane proteins of epithelial cells  in vitro , suggesting that formation of the FrpD-FrpC 1-414  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