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2ja6
From Proteopedia
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CPD LESION CONTAINING RNA POLYMERASE II ELONGATION COMPLEX B
Overview
Cells use transcription-coupled repair (TCR) to efficiently eliminate DNA, lesions such as ultraviolet light-induced cyclobutane pyrimidine dimers, (CPDs). Here we present the structure-based mechanism for the first step, in eukaryotic TCR, CPD-induced stalling of RNA polymerase (Pol) II. A CPD, in the transcribed strand slowly passes a translocation barrier and enters, the polymerase active site. The CPD 5'-thymine then directs uridine, misincorporation into messenger RNA, which blocks translocation., Artificial replacement of the uridine by adenosine enables CPD bypass;, thus, Pol II stalling requires CPD-directed misincorporation. In the, stalled complex, the lesion is inaccessible, and the polymerase, conformation is unchanged. This is consistent with nonallosteric, recruitment of ... [(full description)]
About this Structure
2JA6 is a [Protein complex] structure of sequences from [Saccharomyces cerevisiae] with MG and ZN as [ligands]. Active as [[1]], with EC number [2.7.7.6]. Full crystallographic information is available from [OCA].
Reference
CPD damage recognition by transcribing RNA polymerase II., Brueckner F, Hennecke U, Carell T, Cramer P, Science. 2007 Feb 9;315(5813):859-62. PMID:17290000
Page seeded by OCA on Mon Oct 29 16:00:33 2007
Categories: Protein complex | Saccharomyces cerevisiae | Brueckner, F. | Carell, T. | Cramer, P. | Hennecke, U. | MG | ZN | Arrest | Cpd | Cyclobutane pyrimidine dimer | Damage recognition | Dna damage | Dna lesion | Dna-binding | Dna-directed rna polymerase | Elongation complex | Lesion recognition | Metal-binding | Misincorporation | Nuclear protein | Nucleotidyltransferase | Phosphorylation | Photolesion | Rna polymerase ii | Stalling | Tcr | Thymine dimer | Transcription | Transcription bubble | Transcription- coupled repair | Transferase | Transferase/dna/rna | Zinc | Zinc-finger
