1F08

CRYSTAL STRUCTURE OF THE DNA-BINDING DOMAIN OF THE REPLICATION INITIATION PROTEIN E1 FROM PAPILLOMAVIRUS

Summary for 1F08

• Entry DOI: 10.2210/pdb1f08/pdb
• Descriptor: REPLICATION PROTEIN E1, BROMIDE ION (3 entities in total)
• Functional Keywords: papillomavirus, dna-binding domain, replication, initiator protein, helicase
• Biological source: Bovine papillomavirus
• Cellular location: Host nucleus : P03116
• Total number of polymer chains: 2
• Total formula weight: 34874.20

Authors

Enemark, E.J.,Chen, G.,Vaughn, D.E.,Stenlund, A.,Joshua-Tor, L. (deposition date: 2000-05-15, release date: 2001-05-16, Last modification date: 2024-02-07)

Primary citation

Enemark, E.J.,Chen, G.,Vaughn, D.E.,Stenlund, A.,Joshua-Tor, L.
Crystal structure of the DNA binding domain of the replication initiation protein E1 from papillomavirus.
Mol.Cell, 6:149-158, 2000

PubMed Abstract: 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.

PubMed: 10949036
DOI: 10.1016/S1097-2765(00)00016-2

Experimental method

X-RAY DIFFRACTION (1.9 Å)