2ja8

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[[Category: zinc-finger]]
[[Category: zinc-finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:22:44 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 17:28:17 2007''

Revision as of 15:23, 30 October 2007


2ja8, resolution 3.8Å

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CPD LESION CONTAINING RNA POLYMERASE II ELONGATION COMPLEX D

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

2JA8 is a [Protein complex] structure of sequences from [Saccharomyces cerevisiae] with MG and ZN as [ligands]. Active as [DNA-directed RNA polymerase], with EC number [2.7.7.6]. Structure known Active Site: AC1. 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

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