Structural highlights
Function
[T2D3_HAEIN] Recognizes the double-stranded sequence AAGCTT and cleaves after A-1.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structures of restriction endonuclease HindIII in complex with its cognate DNA and divalent cations.,Watanabe N, Takasaki Y, Sato C, Ando S, Tanaka I Acta Crystallogr D Biol Crystallogr. 2009 Dec;65(Pt 12):1326-33. doi:, 10.1107/S0907444909041134. Epub 2009 Nov 17. PMID:19966419[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Watanabe N, Takasaki Y, Sato C, Ando S, Tanaka I. Structures of restriction endonuclease HindIII in complex with its cognate DNA and divalent cations. Acta Crystallogr D Biol Crystallogr. 2009 Dec;65(Pt 12):1326-33. doi:, 10.1107/S0907444909041134. Epub 2009 Nov 17. PMID:19966419 doi:http://dx.doi.org/10.1107/S0907444909041134
