Summary information and primary citation
- PDB-id
-
1fiu;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- hydrolase-DNA
- Method
- X-ray (1.6 Å)
- Summary
- Tetrameric restriction endonuclease ngomiv in complex
with cleaved DNA
- Reference
-
Deibert M, Grazulis S, Sasnauskas G, Siksnys V, Huber R
(2000): "Structure
of the tetrameric restriction endonuclease NgoMIV in
complex with cleaved DNA." Nat.Struct.Biol.,
7, 792-799. doi: 10.1038/79032.
- Abstract
- The crystal structure of the NgoMIV restriction
endonuclease in complex with cleaved DNA has been
determined at 1.6 A resolution. The crystallographic
asymmetric unit contains a protein tetramer and two DNA
molecules cleaved at their recognition sites. This is the
first structure of a tetrameric restriction enzyme-DNA
complex. In the tetramer, two primary dimers are arranged
back to back with two oligonucleotides bound in clefts on
opposite sides of the tetramer. The DNA molecules retain a
B-type conformation and have an enclosed angle between
their helical axes of 60 degrees. Sequence-specific
interactions occur in both the major and minor grooves. Two
Mg2+ ions are located close to the cleaved phosphate at the
active site of NgoMIV. Biochemical experiments show that
interactions between the recognition sites within the
tetramer greatly increase DNA cleavage efficiency.
