› 1ltl

X-ray diffraction
3Å resolution

THE DODECAMER STRUCTURE OF MCM FROM ARCHAEAL M. THERMOAUTOTROPHICUM

Released:
DOI: 10.2210/pdb1ltl/pdb
PDB entry 1ltl coloured by chain, front view.
PDB entry 1ltl coloured by chain, side view.
PDB entry 1ltl coloured by chain, top view.
Source organism: Methanothermobacter thermautotrophicus
Primary publication:
The structure and function of MCM from archaeal M. Thermoautotrophicum.
Fletcher RJ, Bishop BE, Leon RP, Sclafani RA, Ogata CM, Chen XS
Nat Struct Biol 10 160-7 (2003)
PMID: 12548282

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127916 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA helicase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 279 amino acids
Theoretical weight: 32.34 KDa
Source organism: Methanothermobacter thermautotrophicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O27798 (Residues: 2-275; Coverage: 41%)
Gene name: MTH_1770
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 6 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: R32
Unit cell:
a: 192.321Å b: 192.321Å c: 365.539Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.245 0.245 0.295
Expression system: Escherichia coli

Quick links

Citations

50 review citations

Structure and mechanism of helicases and nucleic acid translocases.
Singleton et al. (2007)
49 more

28 mentions without citation

The origin recognition complex: a biochemical and structural view.
Li et al. (2012)
27 more