Počet záznamů: 1
Structural Basis of Ca2+-Dependent Self-Processing Activity of Repeat-in-Toxin Proteins
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SYSNO ASEP 0524907 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Structural Basis of Ca2+-Dependent Self-Processing Activity of Repeat-in-Toxin Proteins Tvůrce(i) Kubáň, V. (CZ)
Macek, P. (CZ)
Hritz, J. (CZ)
Nechvátalová, K. (CZ)
Nedbalcová, K. (CZ)
Faldyna, M. (CZ)
Šebo, Peter (MBU-M) RID, ORCID
Zídek, L. (CZ)
Bumba, Ladislav (MBU-M) RID, ORCIDČíslo článku e00226-20 Zdroj.dok. mBio. - : American Society for Microbiology - ISSN 2161-2129
Roč. 11, č. 2 (2020)Poč.str. 18 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova RTX toxins ; cell adhesion ; clip-and-link Vědní obor RIV EE - Mikrobiologie, virologie Obor OECD Microbiology CEP GA19-15175S GA ČR - Grantová agentura ČR LM2018133 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Výzkumná infrastruktura CIISB II - 90127 - Masarykova univerzita
CESNET II - 90042 - CESNET - zájmové sdružení právnických osobZpůsob publikování Open access Institucionální podpora MBU-M - RVO:61388971 UT WOS 000531071300056 EID SCOPUS 85081994776 DOI 10.1128/mBio.00226-20 Anotace The posttranslational Ca2+-dependent ´clip-and-link´ activity of large repeat-in-toxin (RTX) proteins starts by Ca2+-dependent structural rearrangement of a highly conserved self-processing module (SPM). Subsequently, an internal aspartate-proline (Asp-Pro) peptide bond at the N-terminal end of SPM breaks, and the liberated C-terminal aspartyl residue can react with a free epsilon-amino group of an adjacent lysine residue to form a new isopeptide bond. Here, we report a solution structure of the calcium-loaded SPM (Ca-SPM) derived from the FrpC protein of Neisseria meningitidis. The Ca-SPM structure defines a unique protein architecture and provides structural insight into the autocatalytic cleavage of the Asp-Pro peptide bond through a ´twisted-amide´ activation. Furthermore, in-frame deletion of the SPM domain from the ApxIVA protein of Actinobacillus pleuropneumoniae attenuated the virulence of this porcine pathogen in a pig respiratory challenge model. We hypothesize that the Ca2+-dependent clip-and-link activity represents an unconventional strategy for Gram-negative pathogens to adhere to the host target cell surface.
IMPORTANCE The Ca2+-dependent clip-and-link activity of large repeat-in-toxin (RTX) proteins is an exceptional posttranslational process in which an internal domain called a self-processing module (SPM) mediates Ca2+ -dependent processing of a highly specific aspartate-proline (Asp-Pro) peptide bond and covalent linkage of the released aspartyl to an adjacent lysine residue through an isopeptide bond. Here, we report the solution structures of the Ca2+-loaded SPM (Ca-SPM) defining the mechanism of the autocatalytic cleavage of the Asp414-Pro415 peptide bond of the Neisseria meningitidis FrpC exoprotein.Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2021 Elektronická adresa https://mbio.asm.org/content/11/2/e00226-20
Počet záznamů: 1