1FIU

TETRAMERIC RESTRICTION ENDONUCLEASE NGOMIV IN COMPLEX WITH CLEAVED DNA

Summary for 1FIU

• Entry DOI: 10.2210/pdb1fiu/pdb
• Descriptor: DNA (5'-D(*TP*GP*CP*G)-3'), DNA (5'-D(P*CP*CP*GP*GP*CP*GP*C)-3'), TYPE II RESTRICTION ENZYME NGOMI, ... (6 entities in total)
• Functional Keywords: protein-dna complex, double helix, restriction endonuclease, restriction-modifiction systems, hydrolase, phosphodiesterase, metal ion, complex (endonuclease-dna), hydrolase-dna complex, hydrolase/dna
• Biological source: Neisseria gonorrhoeae
• Total number of polymer chains: 12
• Total formula weight: 140903.12

Authors

Deibert, M.,Grazulis, S.,Sasnauskas, G.,Siksnys, V.,Huber, R. (deposition date: 2000-08-07, release date: 2001-02-07, Last modification date: 2024-02-07)

Primary citation

Deibert, M.,Grazulis, S.,Sasnauskas, G.,Siksnys, V.,Huber, R.
Structure of the tetrameric restriction endonuclease NgoMIV in complex with cleaved DNA.
Nat.Struct.Biol., 7:792-799, 2000

PubMed 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.

PubMed: 10966652
DOI: 10.1038/79032

Experimental method

X-RAY DIFFRACTION (1.6 Å)