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Title: Crystal Structure of the Simian Virus 40 Large T-Antigen Origin-Binding Domain

Abstract

The origins of replication of DNA tumor viruses have a highly conserved feature, namely, multiple binding sites for their respective initiator proteins arranged as inverted repeats. In the 1.45- Angstroms crystal structure of the simian virus 40 large T-antigen (T-ag) origin-binding domain (obd) reported herein, T-ag obd monomers form a left-handed spiral with an inner channel of 30 Angstroms having six monomers per turn. The inner surface of the spiral is positively charged and includes residues known to bind DNA. Residues implicated in hexamerization of full-length T-ag are located at the interface between adjacent T-ag obd monomers. These data provide a high-resolution model of the hexamer of origin-binding domains observed in electron microscopy studies and allow the obd's to be oriented relative to the hexamer of T-ag helicase domains to which they are connected.

Authors:
; ;
Publication Date:
Research Org.:
Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
914355
Report Number(s):
BNL-78923-2007-JA
Journal ID: ISSN 0022-538X; JOVIAM; TRN: US200809%%197
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Journal Name:
J. Virology
Additional Journal Information:
Journal Volume: 80; Journal ID: ISSN 0022-538X
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; CRYSTAL STRUCTURE; DNA; ELECTRON MICROSCOPY; MONOMERS; ONCOGENIC VIRUSES; PROTEINS; RESIDUES; SIMIAN VIRUS; national synchrotron light source

Citation Formats

Meinke, G, Bullock, P, and Bohm, A. Crystal Structure of the Simian Virus 40 Large T-Antigen Origin-Binding Domain. United States: N. p., 2006. Web. doi:10.1128/JVI.80.9.4304-4312.2006.
Meinke, G, Bullock, P, & Bohm, A. Crystal Structure of the Simian Virus 40 Large T-Antigen Origin-Binding Domain. United States. https://doi.org/10.1128/JVI.80.9.4304-4312.2006
Meinke, G, Bullock, P, and Bohm, A. 2006. "Crystal Structure of the Simian Virus 40 Large T-Antigen Origin-Binding Domain". United States. https://doi.org/10.1128/JVI.80.9.4304-4312.2006.
@article{osti_914355,
title = {Crystal Structure of the Simian Virus 40 Large T-Antigen Origin-Binding Domain},
author = {Meinke, G and Bullock, P and Bohm, A},
abstractNote = {The origins of replication of DNA tumor viruses have a highly conserved feature, namely, multiple binding sites for their respective initiator proteins arranged as inverted repeats. In the 1.45- Angstroms crystal structure of the simian virus 40 large T-antigen (T-ag) origin-binding domain (obd) reported herein, T-ag obd monomers form a left-handed spiral with an inner channel of 30 Angstroms having six monomers per turn. The inner surface of the spiral is positively charged and includes residues known to bind DNA. Residues implicated in hexamerization of full-length T-ag are located at the interface between adjacent T-ag obd monomers. These data provide a high-resolution model of the hexamer of origin-binding domains observed in electron microscopy studies and allow the obd's to be oriented relative to the hexamer of T-ag helicase domains to which they are connected.},
doi = {10.1128/JVI.80.9.4304-4312.2006},
url = {https://www.osti.gov/biblio/914355}, journal = {J. Virology},
issn = {0022-538X},
number = ,
volume = 80,
place = {United States},
year = {Sun Jan 01 00:00:00 EST 2006},
month = {Sun Jan 01 00:00:00 EST 2006}
}