2ja5
From Proteopedia
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|PDB= 2ja5 |SIZE=350|CAPTION= <scene name='initialview01'>2ja5</scene>, resolution 3.8Å | |PDB= 2ja5 |SIZE=350|CAPTION= <scene name='initialview01'>2ja5</scene>, resolution 3.8Å | ||
|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=A:ADENOSINE-5'-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=BRU:5-BROMO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE'>BRU</scene>, <scene name='pdbligand=C:CYTIDINE-5'-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=G:GUANOSINE-5'-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TT:[(1R,3R,4S,9R,10S,12R,15AS,15BR,18BR,18CS)-10-HYDROXY-15A,15B-DIMETHYL-13,15,16,18-TETRAOXOHEXADECAHYDRO-8H-9,12-EPOXY-1,4-METHANO-2,5,7-TRIOXA-12A,14,17,18A-TETRAAZACYCLOHEXADECA[1,2,3,4-DEF]BIPHENYLEN-3-YL]METHYL+DIHYDROGEN+PHOSPHATE'>TT</scene>, <scene name='pdbligand=U:URIDINE-5'-MONOPHOSPHATE'>U</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ja5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ja5 OCA], [http://www.ebi.ac.uk/pdbsum/2ja5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ja5 RCSB]</span> | ||
}} | }} | ||
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[[Category: Cramer, P.]] | [[Category: Cramer, P.]] | ||
[[Category: Hennecke, U.]] | [[Category: Hennecke, U.]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: ZN]] | ||
[[Category: arrest]] | [[Category: arrest]] | ||
[[Category: cpd]] | [[Category: cpd]] | ||
| - | [[Category: cyclobutane pyrimidine dimer]] | ||
[[Category: damage recognition]] | [[Category: damage recognition]] | ||
[[Category: dna damage]] | [[Category: dna damage]] | ||
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[[Category: transcription]] | [[Category: transcription]] | ||
[[Category: transcription bubble]] | [[Category: transcription bubble]] | ||
| - | [[Category: transcription- coupled repair]] | + | [[Category: transcription- coupled repair,cyclobutane pyrimidine dimer]] |
[[Category: transferase]] | [[Category: transferase]] | ||
[[Category: transferase/dna/rna]] | [[Category: transferase/dna/rna]] | ||
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[[Category: zinc-finger]] | [[Category: zinc-finger]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:55:12 2008'' |
Revision as of 00:55, 31 March 2008
| |||||||
| , resolution 3.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , , , , , , , , , | ||||||
| Activity: | DNA-directed RNA polymerase, with EC number 2.7.7.6 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mar 31 03:55:12 2008
Categories: DNA-directed RNA polymerase | Protein complex | Saccharomyces cerevisiae | Brueckner, F. | Carell, T. | Cramer, P. | Hennecke, U. | Arrest | Cpd | 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,cyclobutane pyrimidine dimer | Transferase | Transferase/dna/rna | Zinc | Zinc-finger
