PDBsum entry 6ii2

Toxin

PDB id: 6ii2

Contents

Protein chains

614 a.a.

568 a.a.

539 a.a.

PDB id:

6ii2

Name:

Toxin

Title:

Crystal structure of alpha-beta hydrolase (abh) and makes caterpillars floppy (mcf)-like effectors of vibrio vulnificus mo6-24/o

Structure:

Putative rtx-toxin. Chain: a, b, c, d. Fragment: abh-mcf. Engineered: yes. Mutation: yes

Source:

Vibrio vulnificus. Organism_taxid: 672. Gene: rtxa1. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

3.50Å R-factor: 0.287 R-free: 0.327

Authors:

Y.Lee,B.S.Kim,S.Choi,E.Y.Lee,S.Park,J.Hwang,Y.Kwon,J.Hyung,C.Lee, S.H.Eom,M.H.Kim

Key ref:

Y.Lee et al. (2019). Makes caterpillars floppy-like effector-containing MARTX toxins require host ADP-ribosylation factor (ARF) proteins for systemic pathogenicity. Proc Natl Acad Sci U S A, 116, 18031-18040. PubMed id: 31427506 DOI: 10.1073/pnas.1905095116

Date:

03-Oct-18 Release date: 07-Aug-19

Protein chains

F1CLG9  (F1CLG9_VIBVL) -  Putative RTX-toxin (Fragment) from Vibrio vulnificus

Seq: 1838 a.a.

Struc: 614 a.a.*

Protein chain

F1CLG9  (F1CLG9_VIBVL) -  Putative RTX-toxin (Fragment) from Vibrio vulnificus

Seq: 1838 a.a.

Struc: 568 a.a.*

Protein chain

F1CLG9  (F1CLG9_VIBVL) -  Putative RTX-toxin (Fragment) from Vibrio vulnificus

Seq: 1838 a.a.

Struc: 539 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DOI no: 10.1073/pnas.1905095116

Proc Natl Acad Sci U S A 116:18031-18040 (2019)

PubMed id: 31427506

Makes caterpillars floppy-like effector-containing MARTX toxins require host ADP-ribosylation factor (ARF) proteins for systemic pathogenicity.

Y.Lee, B.S.Kim, S.Choi, E.Y.Lee, S.Park, J.Hwang, Y.Kwon, J.Hyun, C.Lee, J.F.Kim, S.H.Eom, M.H.Kim.

ABSTRACT

Upon invading target cells, multifunctional autoprocessing repeats-in-toxin (MARTX) toxins secreted by bacterial pathogens release their disease-related modularly structured effector domains. However, it is unclear how a diverse repertoire of effector domains within these toxins are processed and activated. Here, we report that Makes caterpillars floppy-like effector (MCF)-containing MARTX toxins require ubiquitous ADP-ribosylation factor (ARF) proteins for processing and activation of intermediate effector modules, which localize in different subcellular compartments following limited processing of holo effector modules by the internal cysteine protease. Effector domains structured tandemly with MCF in intermediate modules become disengaged and fully activated by MCF, which aggressively interacts with ARF proteins present at the same location as intermediate modules and is converted allosterically into a catalytically competent protease. MCF-mediated effector processing leads ultimately to severe virulence in mice via an MCF-mediated ARF switching mechanism across subcellular compartments. This work provides insight into how bacteria take advantage of host systems to induce systemic pathogenicity.