› 3f8t

X-ray diffraction
1.9Å resolution

Crystal structure analysis of a full-length MCM homolog from Methanopyrus kandleri

Released:
DOI: 10.2210/pdb3f8t/pdb
PDB entry 3f8t coloured by chain, front view.
PDB entry 3f8t coloured by chain, side view.
PDB entry 3f8t coloured by chain, top view.
Source organism: Methanopyrus kandleri AV19
Primary publication:
Insights into the architecture of the replicative helicase from the structure of an archaeal MCM homolog.
Bae B, Chen YH, Costa A, Onesti S, Brunzelle JS, Lin Y, Cann IK, Nair SK
Structure 17 211-22 (2009)
PMID: 19217392

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186303 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
MCM domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 506 amino acids
Theoretical weight: 56.63 KDa
Source organism: Methanopyrus kandleri AV19
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8TWB5 (Residues: 1-506; Coverage: 100%)
Gene names: MK1120, mcm2_2
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 42.841Å b: 95.417Å c: 125.374Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.212 0.251
Expression system: Escherichia coli

Quick links

Citations

13 review citations

The Mcm complex: unwinding the mechanism of a replicative helicase.
Bochman et al. (2009)
12 more

6 mentions without citation

Archaeal MCM Proteins as an Analog for the Eukaryotic Mcm2-7 Helicase to Reveal Essential Features of Structure and Function.
Miller et al. (2015)
5 more