Structures of restriction endonuclease HindIII in complex with its cognate DNA and divalent cations.
The three-dimensional crystal structures of HindIII bound to its cognate DNA with and without divalent cations were solved at 2.17 and 2.00 A resolution, respectively. HindIII forms a dimer. The structures showed that HindIII belongs to the EcoRI-like (alpha-class) subfamily of type II restriction endonucleases. The cognate DNA-complex structures revealed the specific DNA-recognition mechanism of HindIII by which it recognizes the palindromic sequence A/AGCTT. In the Mg(2+) ion-soaked structure the DNA was cleaved and two ions were bound at each active site, corresponding to the two-metal-ion mechanism.
Watanabe
Nobuhisa
N
Department of Biotechnology and Biomaterial Chemistry, Graduate School of Engineering, Nagoya University, Japan. nobuhisa@nagoya-u.jp
Takasaki
Yozo
Y
Sato
Chika
C
Ando
Shoji
S
Tanaka
Isao
I
D020134:Catalytic Domain; D002413:Cations, Divalent / Q000737:chemistry; D018360:Crystallography, X-Ray; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D015247:Deoxyribonuclease HindIII / Q000737:chemistry* / Q000378:metabolism; D008274:Magnesium / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary
D002413:Cations, Divalent; D004247:DNA; D015247:Deoxyribonuclease HindIII; D008274:Magnesium