Crystal structure of the DNA binding domain of the replication initiation protein E1 from papillomavirus

Enemark, E. J., Chen, G., Vaughn, D. E., Stenlund, A., Joshua-Tor, L. (July 2000) Crystal structure of the DNA binding domain of the replication initiation protein E1 from papillomavirus. Molecular Cell, 6 (1). pp. 149-158. ISSN 1097-2765 (Public Dataset)

DOI: 10.1016/S1097-2765(05)00016-X


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)-(E-2)(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 Angstrom resolution. Residues critical for DNA binding are located on an extended loop and an a 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 El DNA binding domain orchestrates assembly of the hexameric helicase on the ori.

Item Type: Paper
Uncontrolled Keywords: LARGE T-ANTIGEN Large T-antigen BOVINE PAPILLOMAVIRUS bovine papillomavirus E2 Protein TYPE-1 E1 Type-1 TRANSIENT REPLICATION transient replication TRANSCRIPTION FACTOR transcription factor COMPLEX FORMATION complex formation POLYMERASE ALPHA polymerase alpha VIRAL ORIGIN viral origin HELICASE helicase
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > DNA replication
organism description > virus > papillomavirus
Investigative techniques and equipment > x ray crystallography
CSHL Authors:
Communities: CSHL labs > Joshua-Tor lab
CSHL labs > Stenlund lab
Depositing User: Brian Soldo
Date: July 2000
Date Deposited: 14 Mar 2012 16:54
Last Modified: 05 Sep 2017 19:48
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