› 2in0

X-ray diffraction
1.6Å resolution

crystal structure of Mtu recA intein splicing domain

Released:
DOI: 10.2210/pdb2in0/pdb
PDB entry 2in0 coloured by chain, front view.
PDB entry 2in0 coloured by chain, side view.
PDB entry 2in0 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Crystallographic and mutational studies of Mycobacterium tuberculosis recA mini-inteins suggest a pivotal role for a highly conserved aspartate residue.
Van Roey P, Pereira B, Li Z, Hiraga K, Belfort M, Derbyshire V
J Mol Biol 367 162-73 (2007)
PMID: 17254599

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161555 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endonuclease PI-MtuI Chain: A
Molecule details ›
Chain: A
Length: 139 amino acids
Theoretical weight: 15.42 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WHJ3 (Residues: 252-691; Coverage: 18%)
Gene names: MTV002.02c, Rv2737c, recA
Sequence domains: Intein splicing domain
Structure domains: Hedgehog/Intein (Hint) domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OTHER
Spacegroup: P212121
Unit cell:
a: 36.84Å b: 47.46Å c: 64.63Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.245 0.245 0.275
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Physiology of mycobacteria.
Cook et al. (2009)
5 more

14 mentions without citation

Structural and dynamical features of inteins and implications on protein splicing.
Eryilmaz et al. (2014)
13 more