2ZUG

Crystal structure of WSSV ICP11

Summary for 2ZUG

• Entry DOI: 10.2210/pdb2zug/pdb
• Related: 2GJ2
• Descriptor: ORF115 (WSSV285) (Wsv230) (2 entities in total)
• Functional Keywords: dna mimic protein, dimer, white spot syndrome virus, viral protein
• Biological source: Shrimp white spot syndrome virus (WSSV)
• Total number of polymer chains: 2
• Total formula weight: 20954.23

Authors

Wang, A.H.-J.,Wang, H.-C.,Ko, T.-P.,Lo, C.-F. (deposition date: 2008-10-17, release date: 2008-12-09, Last modification date: 2024-10-30)

Primary citation

Wang, H.-C.,Wang, H.-C.,Ko, T.-P.,Lee, Y.-M.,Leu, J.-H.,Ho, C.-H.,Huang, W.-P.,Lo, C.-F.,Wang, A.H.-J.
White spot syndrome virus protein ICP11: A histone-binding DNA mimic that disrupts nucleosome assembly
Proc.Natl.Acad.Sci.USA, 105:20758-20763, 2008

PubMed Abstract: White spot syndrome virus (WSSV) is a large ( approximately 300 kbp), double-stranded DNA eukaryotic virus that has caused serious disease in crustaceans worldwide. ICP11 is the most highly expressed WSSV nonstructural gene/protein, which strongly suggests its importance in WSSV infection; but until now, its function has remained obscure. We show here that ICP11 acts as a DNA mimic. In crystal, ICP11 formed a polymer of dimers with 2 rows of negatively charged spots that approximated the duplex arrangement of the phosphate groups in DNA. Functionally, ICP11 prevented DNA from binding to histone proteins H2A, H2B, H3, and H2A.x, and in hemocytes from WSSV-infected shrimp, ICP11 colocalized with histone H3 and activated-H2A.x. These observations together suggest that ICP11 might interfere with nucleosome assembly and prevent H2A.x from fulfilling its critical function of repairing DNA double strand breaks. Therefore, ICP11 possesses a functionality that is unique among the handful of presently known DNA mimic proteins.

PubMed: 19095797
DOI: 10.1073/pnas.0811233106

Experimental method

X-RAY DIFFRACTION (2.72 Å)