Structural highlights
Function
[VE1_BPV1] ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Papillomaviral infection causes both benign and malignant lesions and is a necessary cause of cervical carcinoma. Replication of this virus requires the replication initiation proteins E1 and E2, which bind cooperatively at the origin of replication (ori) as an (E1)2-(E2)2-DNA complex. This is a precursor to larger E1 complexes that distort and unwind the ori. We present the crystal structure of the E1 DNA binding domain refined to 1.9 A resolution. Residues critical for DNA binding are located on an extended loop and an alpha helix. We identify the E1 dimerization surface by selective mutations at an E1/E1 interface observed in the crystal and propose a model for the (E1)2-DNA complex. These and other observations suggest how the E1 DNA binding domain orchestrates assembly of the hexameric helicase on the ori.
Crystal structure of the DNA binding domain of the replication initiation protein E1 from papillomavirus.,Enemark EJ, Chen G, Vaughn DE, Stenlund A, Joshua-Tor L Mol Cell. 2000 Jul;6(1):149-58. PMID:10949036[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Enemark EJ, Chen G, Vaughn DE, Stenlund A, Joshua-Tor L. Crystal structure of the DNA binding domain of the replication initiation protein E1 from papillomavirus. Mol Cell. 2000 Jul;6(1):149-58. PMID:10949036
