2jeu | pdb_00002jeu

File:2jeu.jpg

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2jeu, resolution 2.80Å
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TRANSCRIPTION ACTIVATOR STRUCTURE REVEALS REDOX CONTROL OF A REPLICATION INITIATION REACTION

Overview

Redox changes are one of the factors that influence cell-cycle progression and that control the processes of cellular proliferation, differentiation, senescence and apoptosis. Proteins regulated through redox-sensitive cysteines have been characterized but specific 'sulphydryl switches' in replication proteins remain to be identified. In bovine papillomavirus type-1, DNA replication begins when the viral transcription factor E2 recruits the viral initiator protein E1 to the origin of DNA replication (ori). Here we show that a novel dimerization interface in the E2 transcription activation domain is stabilized by a disulphide bond. Oxidative cross-linking via Cys57 sequesters the interaction surface between E1 and E2, preventing pre-initiation and replication initiation complex formation. Our data demonstrate that as well as a mechanism for regulating DNA binding, redox reactions can control replication by modulating the tertiary structure of critical protein factors using a specific redox sensor.

About this Structure

2JEU is a Single protein structure of sequence from Bovine papillomavirus type 1. Full crystallographic information is available from OCA.

Reference

Transcription activator structure reveals redox control of a replication initiation reaction., Sanders CM, Sizov D, Seavers PR, Ortiz-Lombardia M, Antson AA, Nucleic Acids Res. 2007;35(10):3504-15. Epub 2007 May 3. PMID:17478495

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