› 1pm6

Solution NMR

Solution Structure of Full-Length Excisionase (Xis) from Bacteriophage HK022

Released:
DOI: 10.2210/pdb1pm6/pdb
PDB entry 1pm6 coloured by chain, ensemble of 20 models, front view.
PDB entry 1pm6 coloured by chain, ensemble of 20 models, side view.
PDB entry 1pm6 coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia virus HK022
Primary publication:
Solution structure and stability of the full-length excisionase from bacteriophage HK022.
Rogov VV, Lücke C, Muresanu L, Wienk H, Kleinhaus I, Werner K, Löhr F, Pristovsek P, Rüterjans H
Eur J Biochem 270 4846-58 (2003)
PMID: 14653811

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159550 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Excisionase Chain: A
Molecule details ›
Chain: A
Length: 72 amino acids
Theoretical weight: 8.64 KDa
Source organism: Escherichia virus HK022
Expression system: Escherichia coli
UniProt:
  • Canonical: P68927 (Residues: 1-72; Coverage: 100%)
Gene name: xis
Sequence domains: Excisionase-like protein
Structure domains: Multidrug-efflux Transporter Regulator; Chain: A; Domain 2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: energy minimization
Expression system: Escherichia coli

Quick links

Citations

10 citation in other articles

Structure of the cooperative Xis-DNA complex reveals a micronucleoprotein filament that regulates phage lambda intasome assembly.
Abbani et al. (2007)
9 more

1 mention without citation

Diversity of Cultivable Microbes From Soil of the Fildes Peninsula, Antarctica, and Their Potential Application.
Cong et al. (2020)