› 2n9w

Solution NMR

Solution NMR Structure of the membrane localization domain from the Ras/Rap1-specific endopeptidase (RRSP) of the Vibrio vulnificus multifunctional autoprocessing repeats-in-toxins (MARTX) toxin

Released:
DOI: 10.2210/pdb2n9w/pdb
PDB entry 2n9w coloured by chain, ensemble of 20 models, front view.
PDB entry 2n9w coloured by chain, ensemble of 20 models, side view.
PDB entry 2n9w coloured by chain, ensemble of 20 models, top view.
Source organism: Vibrio vulnificus
Primary publication:
The membrane localization domains of two distinct bacterial toxins form a 4-helix-bundle in solution.
Hisao GS, Brothers MC, Ho M, Wilson BA, Rienstra CM
Protein Sci 26 497-504 (2017)
PMID: 27977897

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-104468 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Multifunctional-autoprocessing repeats-in-toxin Chain: A
Molecule details ›
Chain: A
Length: 90 amino acids
Theoretical weight: 10.15 KDa
Source organism: Vibrio vulnificus
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A2S3R7M0 (Residues: 3591-3669; Coverage: 2%)
Gene name: CRN52_02910
Sequence domains: Membrane Localization Domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 79%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

1 review citation

α-Helices in the Type III Secretion Effectors: A Prevalent Feature with Versatile Roles.
Gazi et al. (2021)
2 other articles

2 mentions without citation

Structural basis of inactivation of Ras and Rap1 small GTPases by Ras/Rap1-specific endopeptidase from the sepsis-causing pathogen Vibrio vulnificus.
Jang et al. (2018)
1 more