Volume 88, Issue 1 pp. 106-112
RESEARCH ARTICLE

The structure of the extended E2 DNA-binding domain of the bovine papillomavirus-1

Ludmila Leroy

Ludmila Leroy

Laboratório de Cristalografia, Physics Department, Universidade Federal de Minas Gerais, Belo Horizonte, Brazil

Search for more papers by this author
João Alexandre Ribeiro Gonçalves Barbosa

João Alexandre Ribeiro Gonçalves Barbosa

Laboratory of Molecular Biophysics, Department of Celular Biology, Universidade de Brasília, Brasília, Brazil

Search for more papers by this author
Gonzalo de Prat-Gay

Gonzalo de Prat-Gay

Fundación Instituto Leloir, CABA, Buenos Aires, Argentina

Search for more papers by this author
Igor Polikarpov

Igor Polikarpov

Instituto de Física de São Carlos, Universidade de São Paulo, São Calos, Brazil

Search for more papers by this author
Carlos Basílio Pinheiro

Corresponding Author

Carlos Basílio Pinheiro

Laboratório de Cristalografia, Physics Department, Universidade Federal de Minas Gerais, Belo Horizonte, Brazil

Correspondence

Carlos Basílio Pinheiro, Universidade Federal de Minas Gerais, Departamento de Física – ICEx, Av. Antônio Carlos, 6627, Belo Horizonte 31270-901, Minas Gerais, Brazil.

Email: [email protected]

Search for more papers by this author
First published: 12 July 2019
Citations: 3

Funding information: Conselho Nacional de Desenvolvimento Científico e Tecnológico, Grant/Award Numbers: 309086/2016-7, 477789/2008-0

Abstract

Bovine papillomavirus proteins were extensively studied as a prototype for the human papillomavirus. Here, the crystal structure of the extended E2 DNA-binding domain of the dominant transcription regulator from the bovine papillomavirus strain 1 is described in the space group P3121. We found two protein functional dimers packed in the asymmetric unit. This new protein arrangement inside the crystal led to the reduction of the mobility of a previously unobserved loop directly involved in the protein-DNA interaction, which was then modeled for the first time.

CONFLICT OF INTEREST

The authors declare no conflict of interest.

The full text of this article hosted at iucr.org is unavailable due to technical difficulties.