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PDBsum entry 1adt
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DNA-binding protein
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PDB id
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1adt
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the adenovirus DNA binding protein reveals a hook-On model for cooperative DNA binding.
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Authors
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P.A.Tucker,
D.Tsernoglou,
A.D.Tucker,
F.E.Coenjaerts,
H.Leenders,
P.C.Van der vliet.
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Ref.
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Embo J, 1994,
13,
2994-3002.
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PubMed id
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Abstract
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The adenovirus single-stranded 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. Like other single-stranded DNA binding proteins, it
binds ssDNA, cooperatively. We report the crystal structure, at 2.6 A
resolution, of the nucleic acid binding domain. This domain is active in DNA
replication. The protein contains two zinc atoms in different, novel
coordinations. 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
crystal structure shows that the protein contains a 17 amino acid C-terminal
extension which hooks onto a second molecule, thereby forming a protein chain.
Deletion of this C-terminal arm reduces cooperativity in DNA binding, suggesting
a hook-on model for cooperativity. Based on this structural work and mutant
studies, we propose that DBP forms a protein core around which the
single-stranded DNA winds.
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