The adenovirus early E2A DNA-binding protein (Ad DBP) is a multifunctional protein required, amongst other things, for DNA
replication and transcription control. It binds to single- and double-stranded DNA, as well as to RNA, in a sequence-independent
manner. This signature represents the zinc binding domain of the viral DNA- binding protein, which is active in DNA replication. The zinc atoms appear to be required for the stability of the protein fold rather than being involved in
direct contacts with the DNA, the protein contains two zinc atoms in
different, novel coordinations. Two copies of this domain are found at the C terminus of many members of the family [1].
Kanellopoulos PN, Tsernoglou D, van der Vliet PC, Tucker PA.
Conformational change of the adenovirus DNA-binding protein induced by soaking crystals with K3UO2F5 solutions.
Acta Crystallogr. D Biol. Crystallogr. 52 1996 942-5
[PubMed: 15299602] http://dx.doi.org/10.1107/S0907444996005525
Kanellopoulos PN, Tsernoglou D, van der Vliet PC, Tucker PA.
Alternative arrangements of the protein chain are possible for the adenovirus single-stranded DNA binding protein.
J. Mol. Biol. 257 1996 1-8
[PubMed: 8632448] http://dx.doi.org/10.1006/jmbi.1996.0141