2jeu | pdb_00002jeu

TRANSCRIPTION ACTIVATOR STRUCTURE REVEALS REDOX CONTROL OF A REPLICATION INITIATION REACTION

spinqualitylabelsall models 2jeu, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2jeu is a 1 chain structure with sequence from Bpv-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1dbd, 1jjh, 2bop Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [VE2_BPV1] E2 regulates viral transcription and DNA replication. Binds to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory region. Can either activate or repress transcription depending on E2RE's position with regards to proximal promoter elements. Repression occurs by sterically hindering the assembly of the transcription initiation complex. The E1-E2 complex binds to the origin of DNA replication. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA