1ANV

ADENOVIRUS 5 DBP/URANYL FLUORIDE SOAK

Summary for 1ANV

• Entry DOI: 10.2210/pdb1anv/pdb
• Descriptor: ADENOVIRUS SINGLE-STRANDED DNA-BINDING PROTEIN, ZINC ION, URANYL (VI) ION, ... (4 entities in total)
• Functional Keywords: early protein, dna-binding protein, zinc-finger, phosphorylation, nuclear protein, dna binding protein
• Biological source: Human adenovirus 5
• Cellular location: Host nucleus : P03265
• Total number of polymer chains: 1
• Total formula weight: 41110.68

Authors

Kanellopoulos, P.N.,Tsernoglou, D.,Van Der Vliet, P.C.,Tucker, P.A. (deposition date: 1996-03-14, release date: 1997-02-12, Last modification date: 2024-05-22)

Primary citation

Kanellopoulos, P.N.,Tsernoglou, D.,van der Vliet, P.C.,Tucker, P.A.
Conformational change of the adenovirus DNA-binding protein induced by soaking crystals with K3UO2F5 solutions.
Acta Crystallogr.,Sect.D, 52:942-945, 1996

PubMed Abstract: Soaking crystals of the C-terminal DNA-binding domain of the adenovirus single-stranded DNA-binding protein with a buffer containing K(3)UO(2)F(5) results in a 9% change of the crystallographic c axis without destruction of the crystals or appreciable loss of resolution. The crystals belong to space group P2(1)2(1)2(1) with a = 79.7, b = 75.6 and c = 60.6 A. The three-dimensional structure has been refined to 2.7 A with a crystallographic R factor of 0.206. Antiparallel chains of protein molecules running through the entire crystal are linked by uranyl ions. The relative orientation of protein monomers is flexible, even in the crystalline state, and allows changes in the packing of the protein chains.

PubMed: 15299602
DOI: 10.1107/S0907444996005525

Experimental method

X-RAY DIFFRACTION (2.7 Å)