› 1e5w

X-ray diffraction
2.7Å resolution

Structure of isolated FERM domain and first long helix of moesin

Released:
DOI: 10.2210/pdb1e5w/pdb
PDB entry 1e5w coloured by chain, front view.
PDB entry 1e5w coloured by chain, side view.
PDB entry 1e5w coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The 2.7 A crystal structure of the activated FERM domain of moesin: an analysis of structural changes on activation.
Edwards SD, Keep NH
Biochemistry 40 7061-8 (2001)
PMID: 11401550

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150637 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Moesin Chain: A
Molecule details ›
Chain: A
Length: 346 amino acids
Theoretical weight: 41.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P26038 (Residues: 1-346; Coverage: 60%)
Gene name: MSN
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P42212
Unit cell:
a: 94.36Å b: 94.36Å c: 156.05Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.254 0.254 0.297
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

27 review citations

ERM proteins and merlin: integrators at the cell cortex.
Bretscher et al. (2002)
26 more

11 mentions without citation

Self-masking in an intact ERM-merlin protein: an active role for the central alpha-helical domain.
Li et al. (2007)
10 more