3POV

Crystal structure of a SOX-DNA complex

Summary for 3POV

• Entry DOI: 10.2210/pdb3pov/pdb
• Descriptor: ORF 37, DNA (5'-D(*GP*GP*GP*AP*TP*CP*CP*TP*CP*CP*CP*AP*GP*TP*CP*GP*AP*CP*C)-3'), DNA (5'-D(*GP*GP*TP*CP*GP*AP*CP*TP*AP*GP*GP*AP*GP*GP*AP*TP*CP*CP*C)-3'), ... (6 entities in total)
• Functional Keywords: type ii restriction endonuclease superfamily, nuclease, nucleus/cytoplasm, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Human herpesvirus 8 type M; More
• Total number of polymer chains: 3
• Total formula weight: 67032.05

Authors

Bagneris, C.,Barrett, T.E. (deposition date: 2010-11-23, release date: 2011-09-21, Last modification date: 2023-11-01)

Primary citation

Bagneris, C.,Briggs, L.C.,Savva, R.,Ebrahimi, B.,Barrett, T.E.
Crystal structure of a KSHV-SOX-DNA complex: insights into the molecular mechanisms underlying DNase activity and host shutoff
Nucleic Acids Res., 39:5744-5756, 2011

PubMed Abstract: The early lytic phase of Kaposi's sarcoma herpesvirus infection is characterized by viral replication and the global degradation (shutoff) of host mRNA. Key to both activities is the virally encoded alkaline exonuclease KSHV SOX. While the DNase activity of KSHV SOX is required for the resolution of viral genomic DNA as a precursor to encapsidation, its exact involvement in host shutoff remains to be determined. We present the first crystal structure of a KSHV SOX-DNA complex that has illuminated the catalytic mechanism underpinning both its endo and exonuclease activities. We further illustrate that KSHV SOX, similar to its Epstein-Barr virus homologue, has an intrinsic RNase activity in vitro that although an element of host shutoff, cannot solely account for the phenomenon.

PubMed: 21421561
DOI: 10.1093/nar/gkr111

Experimental method

X-RAY DIFFRACTION (2.5 Å)