› 2a6m

X-ray diffraction
2.4Å resolution

Crystal Structure of the ISHp608 Transposase

Released:
DOI: 10.2210/pdb2a6m/pdb
PDB entry 2a6m coloured by chain, front view.
PDB entry 2a6m coloured by chain, side view.
PDB entry 2a6m coloured by chain, top view.
Source organism: Helicobacter pylori
Primary publication:
Active site sharing and subterminal hairpin recognition in a new class of DNA transposases.
Ronning DR, Guynet C, Ton-Hoang B, Perez ZN, Ghirlando R, Chandler M, Dyda F
Mol Cell 20 143-54 (2005)
PMID: 16209952

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-188010 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transposase IS200-like domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 155 amino acids
Theoretical weight: 18.11 KDa
Source organism: Helicobacter pylori
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q933Z0 (Residues: 1-155; Coverage: 100%)
Gene names: B0X28_06285, B0X28_06415, B0X28_06965, B0X28_07035, B0X28_07355, B0X28_07380, B0X28_07400, B0X28_07410, B0X28_08670, B0X29_00655, B0X39_04170, BB413_07925, BB437_07715, DD756_06260, DDP35_01150, DDP42_08030, EC527_06560, EC565_08270, EPC71_00690, EPC72_02395, tnpA
Sequence domains: Transposase IS200 like
Structure domains: Transposase IS200-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200, APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 124.52Å b: 50.976Å c: 52.921Å
α: 90° β: 105.45° γ: 90°
R-values:
R R work R free
0.254 0.254 0.272
Expression system: Escherichia coli BL21(DE3)

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Citations

11 review citations

ISCR elements: novel gene-capturing systems of the 21st century?
Toleman et al. (2006)
10 more

5 mentions without citation

The processing of repetitive extragenic palindromes: the structure of a repetitive extragenic palindrome bound to its associated nuclease.
Messing et al. (2012)
4 more