2fuf
From Proteopedia
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Crystal structure of the SV40 large T antigen origin-binding domain
Overview
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.
About this Structure
2FUF is a Single protein structure of sequence from Simian virus 40 with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the simian virus 40 large T-antigen origin-binding domain., Meinke G, Bullock PA, Bohm A, J Virol. 2006 May;80(9):4304-12. PMID:16611889
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