2ja5
From Proteopedia
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| - | [[Image:2ja5.jpg|left|200px]]<br /><applet load="2ja5" size=" | + | [[Image:2ja5.jpg|left|200px]]<br /><applet load="2ja5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ja5, resolution 3.8Å" /> | caption="2ja5, resolution 3.8Å" /> | ||
'''CPD LESION CONTAINING RNA POLYMERASE II ELONGATION COMPLEX A'''<br /> | '''CPD LESION CONTAINING RNA POLYMERASE II ELONGATION COMPLEX A'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2JA5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with MG and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] Known structural/functional Site: <scene name='pdbsite=AC1:Zn Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2JA5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] Known structural/functional Site: <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JA5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zinc-finger]] | [[Category: zinc-finger]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:43:21 2008'' |
Revision as of 08:43, 3 February 2008
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CPD LESION CONTAINING RNA POLYMERASE II ELONGATION COMPLEX A
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 repair factors and excision of a lesion-containing DNA, fragment in the presence of Pol II.
About this Structure
2JA5 is a Protein complex structure of sequences from Saccharomyces cerevisiae with and as ligands. Active as DNA-directed RNA polymerase, with EC number 2.7.7.6 Known structural/functional Site: . 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 Sun Feb 3 10:43:21 2008
Categories: DNA-directed RNA polymerase | 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
