1EV7

CRYSTAL STRUCTURE OF DNA RESTRICTION ENDONUCLEASE NAEI

Summary for 1EV7

• Entry DOI: 10.2210/pdb1ev7/pdb
• Descriptor: TYPE IIE RESTRICTION ENDONUCLEASE NAEI (2 entities in total)
• Functional Keywords: apo-naei, restriction endonuclease, topoisomerase, helix-turn-helix, cap, hydrolase
• Biological source: Lechevalieria aerocolonigenes
• Total number of polymer chains: 2
• Total formula weight: 70768.06

Authors

Huai, Q.,Colandene, J.D.,Chen, Y.,Luo, F.,Zhao, Y. (deposition date: 2000-04-19, release date: 2000-10-19, Last modification date: 2024-02-07)

Primary citation

Huai, Q.,Colandene, J.D.,Chen, Y.,Luo, F.,Zhao, Y.,Topal, M.D.,Ke, H.
Crystal structure of NaeI-an evolutionary bridge between DNA endonuclease and topoisomerase.
EMBO J., 19:3110-3118, 2000

PubMed Abstract: NAE:I is transformed from DNA endonuclease to DNA topoisomerase and recombinase by a single amino acid substitution. The crystal structure of NAE:I was solved at 2.3 A resolution and shows that NAE:I is a dimeric molecule with two domains per monomer. Each domain contains one potential DNA recognition motif corresponding to either endonuclease or topoisomerase activity. The N-terminal domain core folds like the other type II restriction endonucleases as well as lambda-exonuclease and the DNA repair enzymes MutH and Vsr, implying a common evolutionary origin and catalytic mechanism. The C-terminal domain contains a catabolite activator protein (CAP) motif present in many DNA-binding proteins, including the type IA and type II topoisomerases. Thus, the NAE:I structure implies that DNA processing enzymes evolved from a few common ancestors. NAE:I may be an evolutionary bridge between endonuclease and DNA processing enzymes.

PubMed: 10856254
DOI: 10.1093/emboj/19.12.3110

Experimental method

X-RAY DIFFRACTION (2.38 Å)