A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä
1H, 13C, and 15N NMR chemical shift assignment of the complex formed by the first EPEC EspF repeat and N-WASP GTPase binding domain (2021)


Karjalainen, M., Hellman, M., Tossavainen, H., & Permi, P. (2021). 1H, 13C, and 15N NMR chemical shift assignment of the complex formed by the first EPEC EspF repeat and N-WASP GTPase binding domain. Biomolecular NMR Assignments, 15(1), 213-217. https://doi.org/10.1007/s12104-021-10008-9


JYU-tekijät tai -toimittajat


Julkaisun tiedot

Julkaisun kaikki tekijät tai toimittajatKarjalainen, Mikael; Hellman, Maarit; Tossavainen, Helena; Permi, Perttu

Lehti tai sarjaBiomolecular NMR Assignments

ISSN1874-2718

eISSN1874-270X

Julkaisuvuosi2021

Ilmestymispäivä21.01.2021

Volyymi15

Lehden numero1

Artikkelin sivunumerot213-217

KustantajaSpringer

JulkaisumaaAlankomaat

Julkaisun kielienglanti

DOIhttps://doi.org/10.1007/s12104-021-10008-9

Julkaisun avoin saatavuusAvoimesti saatavilla

Julkaisukanavan avoin saatavuusOsittain avoin julkaisukanava

Julkaisu on rinnakkaistallennettu (JYX)https://jyx.jyu.fi/handle/123456789/73852


Tiivistelmä

LEE-encoded effector EspF (EspF) is an effector protein part of enteropathogenic Escherichia coli’s (EPEC’s) arsenal for intestinal infection. This intrinsically disordered protein contains three highly conserved repeats which together compose over half of the protein’s complete amino acid sequence. EPEC uses EspF to hijack host proteins in order to promote infection. In the attack EspF is translocated, together with other effector proteins, to host cell via type III secretion system. Inside host EspF stimulates actin polymerization by interacting with Neural Wiskott-Aldrich syndrome protein (N-WASP), a regulator in actin polymerization machinery. It is presumed that EspF acts by disrupting the autoinhibitory state of N-WASP GTPase binding domain. In this NMR spectroscopy study, we report the 1H, 13C, and 15N resonance assignments for the complex formed by the first 47-residue repeat of EspF and N-WASP GTPase binding domain. These near-complete resonance assignments provide the basis for further studies which aim to characterize structure, interactions, and dynamics between these two proteins in solution.


YSO-asiasanatproteiinitNMR-spektroskopia

Vapaat asiasanatEPEC EspF; intrinsically disordered protein; N-WASP; resonance assignments; solution NMR; type III secretion system


Liittyvät organisaatiot


Hankkeet, joissa julkaisu on tehty


OKM-raportointiKyllä

Raportointivuosi2021

JUFO-taso1


Viimeisin päivitys 2024-26-03 klo 20:56