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Structure paper

TitleStructure, subunit organization and behavior of the asymmetric Type IIT restriction endonuclease BbvCI.
Journal, issue, pagesNucleic Acids Res., Vol. 47, Page 450-467, Year 2019
Publish dateAug 19, 2018 (structure data deposition date)
AuthorsShen, B.W. / Doyle, L. / Bradley, P. / Heiter, D.F. / Lunnen, K.D. / Wilson, G.G. / Stoddard, B.L.
External linksNucleic Acids Res. / PubMed:30395313
MethodsX-ray diffraction
Resolution2.07 - 3.79 Å
Structure data

PDB-6eg7:
BbvCI B2 dimer with I3C clusters
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-6m9g:
BbvCI B2 dimer with Ta6Br14 clusters
Method: X-RAY DIFFRACTION / Resolution: 2.35 Å

PDB-6maf:
native BbvCI A2B2 tetramer at low resolution
Method: X-RAY DIFFRACTION / Resolution: 3.79 Å

PDB-6mag:
native BbvCI B2 dimer in space group C222
Method: X-RAY DIFFRACTION / Resolution: 2.07 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-I3C:
5-amino-2,4,6-triiodobenzene-1,3-dicarboxylic acid

ChemComp-HOH:
WATER

ChemComp-TBR:
HEXATANTALUM DODECABROMIDE

ChemComp-BR:
BROMIDE ION

ChemComp-SO4:
SULFATE ION

ChemComp-ACT:
ACETATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-PO4:
PHOSPHATE ION

Source
  • brevibacillus brevis (bacteria)
KeywordsHYDROLASE / endonuclease / DNA binding protein / Type IIT restriction enzyme

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