1BY9

CRYSTAL STRUCTURE OF THE E2 DNA-BINDING DOMAIN FROM HUMAN PAPILLOMAVIRUS TYPE-16: IMPLICATIONS FOR ITS DNA BINDING-SITE SELECTION MECHANISM

1BY9 の概要

• エントリーDOI: 10.2210/pdb1by9/pdb
• 分子名称: REGULATORY PROTEIN E2 (2 entities in total)
• 機能のキーワード: papillomavirus, transcription regulation, beta-barrel
• 由来する生物種: Human papillomavirus type 16
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9368.82

構造登録者

Hegde, R.S.,Androphy, E.J. (登録日: 1998-10-27, 公開日: 1999-04-27, 最終更新日: 2024-05-22)

主引用文献

Hegde, R.S.,Androphy, E.J.
Crystal structure of the E2 DNA-binding domain from human papillomavirus type 16: implications for its DNA binding-site selection mechanism.
J.Mol.Biol., 284:1479-1489, 1998

PubMed Abstract: The crystal structure of the E2 DNA-binding domain from the high-risk cervical cancer-associated strain human papillomavirus type 16 (HPV-16) is described here. The papillomavirus E2 proteins regulate transcription from all viral promoters and are required for the initiation of replication in vivo. They belong to a family of viral proteins that form dimeric beta-barrels and use surface alpha-helices for DNA interaction. Although all E2 proteins recognize the same consensus, palindromic DNA sequence, proteins from different viral strains differ in their abilities to discriminate among their specific DNA-binding sites. The structure reported here reveals that while the overall fold of the HPV-16 E2 DNA-binding domain resembles that of its counterpart from the related viral strain bovine papillomavirus type 1, the precise placement of the recognition helices is significantly different. Additionally, the charge distribution on the DNA-binding surfaces of the two proteins varies; HPV-16 E2 has a much less electropositive surface. HPV-16 E2 is thus less able to utilize charge neutralization of the phosphate groups on DNA to induce bending. These results correlate well with previous solution studies that showed decreased affinity between HPV-16 E2 and flexible DNA target sequences, and enhanced affinity towards A-tract-containing, pre-bent sequences. In summary, the crystal structure of the HPV-16 E2 DNA-binding domain shows that the protein presents a stereo-chemically and electrostatically unique surface to DNA, characteristics that can contribute to its mechanism of DNA target discrimination.

PubMed: 9878365
DOI: 10.1006/jmbi.1998.2260

実験手法

X-RAY DIFFRACTION (2.2 Å)