4cwm: Difference between revisions
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/ENDO2_ARATH ENDO2_ARATH]] Probable endonuclease (By similarity). Can not hydrolyze single stranded DNA and does not cleave mismatches. | [[http://www.uniprot.org/uniprot/ENDO2_ARATH ENDO2_ARATH]] Probable endonuclease (By similarity). Can not hydrolyze single stranded DNA and does not cleave mismatches. | ||
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== Publication Abstract from PubMed == | |||
The multi S1/P1 nuclease AtBFN2 (EC 3.1.30.1) encoded by the Arabidopsis thaliana At1g68290 gene is a glycoprotein that digests RNA, ssDNA, and dsDNA. AtBFN2 depends on three zinc ions for cleaving DNA and RNA at 3'-OH to yield 5'-nucleotides. In addition, AtBFN2's enzymatic activity is strongly glycan dependent. Plant Zn(2+)-dependent endonucleases present a unique fold, and belong to the Phospholipase C (PLC)/P1 nuclease superfamily. In this work, we present the first complete, ligand-free, AtBFN2 crystal structure, along with sulfate, phosphate and ssDNA co-crystal structures. With these, we were able to provide better insight into the glycan structure and possible enzymatic mechanism. In comparison with other nucleases, the AtBFN2/ligand-free and AtBFN2/PO4 models suggest a similar, previously proposed, catalytic mechanism. Our data also confirm that the phosphate and vanadate can inhibit the enzyme activity by occupying the active site. More importantly, the AtBFN2/A5T structure reveals a novel and conserved secondary binding site, which seems to be important for plant Zn(2+)-dependent endonucleases. Based on these findings, we propose a rational ssDNA binding model, in which the ssDNA wraps itself around the protein and the attached surface glycan, in turn, reinforces the binding complex. | |||
Structural insights of the ssDNA binding site in the multifunctional endonuclease AtBFN2 from Arabidopsis thaliana.,Yu TF, Maestre-Reyna M, Ko CY, Ko TP, Sun YJ, Lin TY, Shaw JF, Wang AH PLoS One. 2014 Aug 26;9(8):e105821. doi: 10.1371/journal.pone.0105821., eCollection 2014. PMID:25157844<ref>PMID:25157844</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
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</StructureSection> | </StructureSection> | ||