Structural basis of the interaction between the putative adhesion-involved and iron-regulated FrpD and FrpC proteins of Neisseria meningitidis

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F17%3A43895564" target="_blank" >RIV/60076658:12310/17:43895564 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/17:00473584 RIV/68378050:_____/17:00473584 RIV/61388963:_____/17:00474984

Výsledek na webu

<a href="https://www.nature.com/articles/srep40408.pdf" target="_blank" >https://www.nature.com/articles/srep40408.pdf</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/srep40408" target="_blank" >10.1038/srep40408</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Structural basis of the interaction between the putative adhesion-involved and iron-regulated FrpD and FrpC proteins of Neisseria meningitidis

Popis výsledku v původním jazyce

The iron-regulated protein FrpD from Neisseria meningitidis is an outer membrane lipoprotein that interacts with very high affinity (K-d similar to 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 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.

Název v anglickém jazyce

Structural basis of the interaction between the putative adhesion-involved and iron-regulated FrpD and FrpC proteins of Neisseria meningitidis

Popis výsledku anglicky

The iron-regulated protein FrpD from Neisseria meningitidis is an outer membrane lipoprotein that interacts with very high affinity (K-d similar to 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 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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

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OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2017

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Scientific Reports

ISSN

2045-2322

e-ISSN

—

Svazek periodika

7

Číslo periodika v rámci svazku

JAN 13 2017

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

14

Strana od-do

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Kód UT WoS článku

000392190700001

EID výsledku v databázi Scopus

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