2CO5

F93 FROM STIV, a winged-helix DNA-binding protein

Summary for 2CO5

• Entry DOI: 10.2210/pdb2co5/pdb
• Descriptor: VIRAL PROTEIN F93 (2 entities in total)
• Functional Keywords: viral protein-winged helix complex, winged helix, dna-binding, hth, whth, f93, disulfide bond, stiv, sulfolobus turreted icosahedral virus, viral protein, virus, archaea, crenarchaea, archaeal virus, crenarchaeal virus, thermophilic protein, thermophilic virus, sulfolobus, yellowstone, viral protein/winged helix
• Biological source: SULFOLOBUS TURRETED ICOSAHEDRAL VIRUS (STIV)
• Total number of polymer chains: 2
• Total formula weight: 24000.37

Authors

Larson, E.T.,Reiter, D.,Lawrence, C.M. (deposition date: 2006-05-25, release date: 2006-05-31, Last modification date: 2024-10-23)

Primary citation

Larson, E.T.,Eilers, B.,Menon, S.,Reiter, D.,Ortmann, A.,Young, M.J.,Lawrence, C.M.
A Winged-Helix Protein from Sulfolobus Turreted Icosahedral Virus Points Toward Stabilizing Disulfide Bonds in the Intracellular Proteins of a Hyperthermophilic Virus.
Virology, 368:249-, 2007

PubMed Abstract: Sulfolobus turreted icosahedral virus (STIV) was the first non-tailed icosahedral virus to be isolated from an archaeal host. Like other archaeal viruses, its 37 open reading frames generally lack sequence similarity to genes with known function. The roles of the gene products in this and other archaeal viruses are thus largely unknown. However, a protein's three-dimensional structure may provide functional and evolutionary insight in cases of minimal sequence similarity. In this vein, the structure of STIV F93 reveals a homodimer with strong similarity to the winged-helix family of DNA-binding proteins. Importantly, an interchain disulfide bond is found at the dimer interface, prompting analysis of the cysteine distribution in the putative intracellular proteins of the viral proteome. The analysis suggests that intracellular disulfide bonds are common in cellular STIV proteins, where they enhance the thermostability of the viral proteome.

PubMed: 17669459
DOI: 10.1016/J.VIROL.2007.06.040

Experimental method

X-RAY DIFFRACTION (2.2 Å)