Database accession: MF2120024
Name: Antitoxin phd dimer (Mycobacterium tuberculosis)
PDB ID: 3g5o
Experimental method: X-ray (2.00 Å)
Assembly: homodimer
Source organism: Mycobacterium tuberculosis
Primer publication of the structure:
Miallau, L., Chernishof, I., Chiang, J., Arbing, M., Cascio, D., Eisenberg, D.;
The crystal structure of the toxin-antitoxin complex RelBE2 (Rv2865-2866) from Mycobacterium tuberculosis
To be published...
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
toxin-antitoxin pair type II binding Interacting selectively and non-covalently with a toxic protein, disabling its function. There may be more than one antitoxin to a toxic protein. Instances of this activity are known only in prokaryotes, where the toxic protein may be a ribonuclease, a DNA gyrase, or other.
Biological process:
regulation of transcription, DNA-templated Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
positive regulation of growth Any process that activates or increases the rate or extent of growth, the increase in size or mass of all or part of an organism.
transcription, DNA-templated The cellular synthesis of RNA on a template of DNA.
Cellular component: not assigned
Structural annotations of the participating protein chains.Entry contents: 2 distinct polypeptide molecules
Chains: A, D
Notes: Chains B and C were removed as chains A and D represent the biologically relevant dimer. Chains A and D were truncated to exclude the regions in contact with chains B and C.
Number of unique protein segments: 1
Name: Antitoxin RelF
Source organism: Mycobacterium tuberculosis
Length: 93 residues
Sequence:Sequence according to PDB SEQRESMRILPISTIKGKLNEFVDAVSSTQDQITITKNGAPAAVLVGADEWESLQETLYWLAQPGIRESIAEADADIASGRTYGEDEIRAEFGVPRRPH
UniProtKB AC: O33347 (positions: 1-93) Coverage: 100%
UniRef90 AC: UniRef90_O33347 (positions: 1-93)
Name: Antitoxin RelF
Source organism: Mycobacterium tuberculosis
Length: 93 residues
Sequence:Sequence according to PDB SEQRESMRILPISTIKGKLNEFVDAVSSTQDQITITKNGAPAAVLVGADEWESLQETLYWLAQPGIRESIAEADADIASGRTYGEDEIRAEFGVPRRPH
UniProtKB AC: O33347 (positions: 1-93) Coverage: 100%
UniRef90 AC: UniRef90_O33347 (positions: 1-93)
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Complex evidence:
The dimerization of the prevents host death (phd) antitoxin from Escherichia virus P1 has been shown with differential scanning calorimetry to fit well to a two-state model consisting of a dimer unfolding into monomer species (PMID: 20603017).
Chain A:
A homologue sharing the same Pfam domain (PF02604.16) has been experimentally characterized as disordered in DisProt entry DP00288.
Chain D:
A homologue sharing the same Pfam domain (PF02604.16) has been experimentally characterized as disordered in DisProt entry DP00288.
Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap). No related structure was found in the Protein Data Bank.
Download our modified structure (.pdb)
