3WAZ

Crystal structure of a restriction enzyme PabI in complex with DNA

Summary for 3WAZ

• Entry DOI: 10.2210/pdb3waz/pdb
• Related: 2DVY
• Descriptor: Putative uncharacterized protein, DNA (5'-D(*GP*CP*AP*TP*AP*GP*CP*TP*GP*TP*(ORP)P*CP*AP*GP*CP*TP*AP*TP*GP*C)-3'), ADENINE (3 entities in total)
• Functional Keywords: restriction enzyme, dna binding, hydrolase-dna complex, hydrolase/dna
• Biological source: Pyrococcus abyssi; More
• Total number of polymer chains: 4
• Total formula weight: 62984.26

Authors

Miyazono, K.,Miyakawa, T.,Ito, T.,Tanokura, M. (deposition date: 2013-05-10, release date: 2014-01-29, Last modification date: 2023-11-08)

Primary citation

Miyazono, K.,Furuta, Y.,Watanabe-Matsui, M.,Miyakawa, T.,Ito, T.,Kobayashi, I.,Tanokura, M.
A sequence-specific DNA glycosylase mediates restriction-modification in Pyrococcus abyssi.
Nat Commun, 5:3178-3178, 2014

PubMed Abstract: Restriction-modification systems consist of genes that encode a restriction enzyme and a cognate methyltransferase. Thus far, it was believed that restriction enzymes are sequence-specific endonucleases that introduce double-strand breaks at specific sites by catalysing the cleavages of phosphodiester bonds. Here we report that based on the crystal structure and enzymatic activity, one of the restriction enzymes, R.PabI, is not an endonuclease but a sequence-specific adenine DNA glycosylase. The structure of the R.PabI-DNA complex shows that R.PabI unwinds DNA at a 5'-GTAC-3' site and flips the guanine and adenine bases out of the DNA helix to recognize the sequence. R.PabI catalyses the hydrolysis of the N-glycosidic bond between the adenine base and the sugar in the DNA and produces two opposing apurinic/apyrimidinic (AP) sites. The opposing AP sites are cleaved by heat-promoted β elimination and/or by endogenous AP endonucleases of host cells to introduce a double-strand break.

PubMed: 24458096
DOI: 10.1038/ncomms4178

Experimental method

X-RAY DIFFRACTION (3 Å)