› 2lsm

Solution NMR

Solution structure of gpFI C-terminal domain

Released:
DOI: 10.2210/pdb2lsm/pdb
PDB entry 2lsm coloured by chain, ensemble of 20 models, front view.
PDB entry 2lsm coloured by chain, ensemble of 20 models, side view.
PDB entry 2lsm coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia virus Lambda
Primary publication:
Structural and biochemical characterization of phage λ FI protein (gpFI) reveals a novel mechanism of DNA packaging chaperone activity.
Popovic A, Wu B, Arrowsmith CH, Edwards AM, Davidson AR, Maxwell KL
J Biol Chem 287 32085-95 (2012)
PMID: 22801427

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137220 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA-packaging protein FI Chain: A
Molecule details ›
Chain: A
Length: 61 amino acids
Theoretical weight: 6.5 KDa
Source organism: Escherichia virus Lambda
Expression system: Escherichia coli
UniProt:
  • Canonical: P03709 (Residues: 72-132; Coverage: 46%)
Gene names: Fi, lambdap09
Sequence domains: DNA packaging protein FI
Structure domains: DNA packaging chaperone protein FI, C-terminal beta-strand domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 82%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

6 citation in other articles

HNH proteins are a widespread component of phage DNA packaging machines.
Kala et al. (2014)
5 more

1 mention without citation

Structural and biochemical characterization of phage λ FI protein (gpFI) reveals a novel mechanism of DNA packaging chaperone activity.
Popovic et al. (2012)