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Structure paper

TitleStructures of minimal catalytic fragments of topoisomerase v reveals conformational changes relevant for DNA binding.
Journal, issue, pagesStructure, Vol. 18, Page 829-838, Year 2010
Publish dateMar 15, 2010 (structure data deposition date)
AuthorsRajan, R. / Taneja, B. / Mondragon, A.
External linksStructure / PubMed:20637419
MethodsX-ray diffraction
Resolution1.4 - 2.6 Å
Structure data

PDB-3m6k:
Crystal Structure of N-terminal 44 kDa fragment of topoisomerase V in the presence of guanidium hydrochloride
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-3m6z:
Crystal structure of an N-terminal 44 kDa fragment of topoisomerase V in the presence of guanidium hydrochloride
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-3m7d:
Crystal structure of an N-terminal 44 kDA fragment of topoisomerase V in the presence of dioxane
Method: X-RAY DIFFRACTION / Resolution: 1.815 Å

PDB-3m7g:
Structure of topoisomerase domain of topoisomerase V protein
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-GAI:
GUANIDINE

Source
  • methanopyrus kandleri (archaea)
KeywordsISOMERASE / helix-hairpin-helix / topoisomerase / conformational change in protein / guanidium hydrochloride / conformational changes in protein / conformational change / topoisomerase V / type IC topoisomerase / minimal catalytic fragment of topoisomerase V

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