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Structure paper

TitleThe Structural Basis of Asymmetry in DNA Binding and Cleavage as Exhibited by the I-SmaMI LAGLIDADG Meganuclease.
Journal, issue, pagesJ. Mol. Biol., Vol. 428, Page 206-220, Year 2016
Publish dateOct 8, 2015 (structure data deposition date)
AuthorsShen, B.W. / Lambert, A. / Walker, B.C. / Stoddard, B.L. / Kaiser, B.K.
External linksJ. Mol. Biol. / PubMed:26705195
MethodsX-ray diffraction
Resolution2.2 - 2.65 Å
Structure data

PDB-5e5o:
I-SmaMI bound to uncleaved DNA target in the presence of Calcium ions
Method: X-RAY DIFFRACTION / Resolution: 2.36 Å

PDB-5e5p:
Wild type I-SmaMI in the space group of C121
Method: X-RAY DIFFRACTION / Resolution: 2.65 Å

PDB-5e5s:
I-SmaMI K103A mutant
Method: X-RAY DIFFRACTION / Resolution: 2.29 Å

PDB-5e63:
K262A mutant of I-SmaMI
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-5e67:
K103A/K262A double mutant of I-SmaMI
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-PG0:
2-(2-METHOXYETHOXY)ETHANOL / inhibitor, precipitant*YM

ChemComp-MG:
Unknown entry

ChemComp-MXE:
2-METHOXYETHANOL

Source
  • sordaria macrospora (strain atcc mya-333 / dsm 997 / k(l3346) / k-hell) (fungus)
  • synthetic construct (others)
KeywordsHYDROLASE/DNA / LAGLIDADG / I-SmaMI / Complex / uncleaved / HYDROLASE-DNA complex / HYDROLASE / I-SmaMI mutant / nickase / K262A / mutant / K103A/K262A

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