5DWC

Crystal structure of restriction endonuclease AgeI

Summary for 5DWC

• Entry DOI: 10.2210/pdb5dwc/pdb
• Descriptor: Type-2 restriction enzyme AgeI (2 entities in total)
• Functional Keywords: restriction endonuclease, pd-(d/e)xk nuclease, hydrolase
• Biological source: Thalassobius gelatinovorus
• Total number of polymer chains: 1
• Total formula weight: 30593.52

Authors

Tamulaitiene, G.,Ramonaite, I.,Grazulis, S.,Siksnys, V. (deposition date: 2015-09-22, release date: 2016-09-28, Last modification date: 2024-11-13)

Primary citation

Tamulaitiene, G.,Jovaisaite, V.,Tamulaitis, G.,Songailiene, I.,Manakova, E.,Zaremba, M.,Grazulis, S.,Xu, S.Y.,Siksnys, V.
Restriction endonuclease AgeI is a monomer which dimerizes to cleave DNA.
Nucleic Acids Res., 45:3547-3558, 2017

PubMed Abstract: Although all Type II restriction endonucleases catalyze phosphodiester bond hydrolysis within or close to their DNA target sites, they form different oligomeric assemblies ranging from monomers, dimers, tetramers to higher order oligomers to generate a double strand break in DNA. Type IIP restriction endonuclease AgeI recognizes a palindromic sequence 5΄-A/CCGGT-3΄ and cuts it ('/' denotes the cleavage site) producing staggered DNA ends. Here, we present crystal structures of AgeI in apo and DNA-bound forms. The structure of AgeI is similar to the restriction enzymes that share in their target sites a conserved CCGG tetranucleotide and a cleavage pattern. Structure analysis and biochemical data indicate, that AgeI is a monomer in the apo-form both in the crystal and in solution, however, it binds and cleaves the palindromic target site as a dimer. DNA cleavage mechanism of AgeI is novel among Type IIP restriction endonucleases.

PubMed: 28039325
DOI: 10.1093/nar/gkw1310

Experimental method

X-RAY DIFFRACTION (2.5 Å)