6bus

Extended E2 DNA-binding domain of the Bovine Papillomavirus-1Extended E2 DNA-binding domain of the Bovine Papillomavirus-1

Structural highlights 6bus is a 4 chain structure with sequence from Deltapapillomavirus 4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function VE2_BPV1 E2 regulates viral transcription and DNA replication. Binds to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory region. Can either activate or repress transcription depending on E2RE's position with regards to proximal promoter elements. Repression occurs by sterically hindering the assembly of the transcription initiation complex. The E1-E2 complex binds to the origin of DNA replication. Publication Abstract from PubMed 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 P31 21. 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 modelled for the first time. This article is protected by copyright. All rights reserved. The structure of the extended E2 DNA-binding domain of the Bovine Papillomavirus-1.,Leroy LMD, Barbosa JARG, de Prat-Gay G, Polikarpov I, Pinheiro CB Proteins. 2019 Jul 12. doi: 10.1002/prot.25773. PMID:31299114 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Regulatory protein E2

spinqualitylabelsall models 6bus, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image