2W8M
Structure of D212, a nuclease from a fusselovirus.
Summary for 2W8M
Entry DOI | 10.2210/pdb2w8m/pdb |
Descriptor | ORF D212 (2 entities in total) |
Functional Keywords | ssv1, crenarchaeal virus, hydrolase |
Biological source | SULFOLOBUS VIRUS RAGGED HILLS |
Total number of polymer chains | 2 |
Total formula weight | 50213.44 |
Authors | Menon, S.K.,Young, M.J.,Lawrence, C.M. (deposition date: 2009-01-17, release date: 2009-02-03, Last modification date: 2024-05-08) |
Primary citation | Menon, S.K.,Eilers, B.J.,Young, M.J.,Lawrence, C.M. The crystal structure of D212 from sulfolobus spindle-shaped virus ragged hills reveals a new member of the PD-(D/E)XK nuclease superfamily. J. Virol., 84:5890-5897, 2010 Cited by PubMed Abstract: Structural studies have made significant contributions to our understanding of Sulfolobus spindle-shaped viruses (Fuselloviridae), an important model system for archaeal viruses. Continuing these efforts, we report the structure of D212 from Sulfolobus spindle-shaped virus Ragged Hills. The overall fold and conservation of active site residues place D212 in the PD-(D/E)XK nuclease superfamily. The greatest structural similarity is found to the archaeal Holliday junction cleavage enzymes, strongly suggesting a role in DNA replication, repair, or recombination. Other roles associated with nuclease activity are also considered. PubMed: 20375162DOI: 10.1128/JVI.01663-09 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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