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2VUM

Alpha-amanitin inhibited complete RNA polymerase II elongation complex

Summary for 2VUM
Entry DOI10.2210/pdb2vum/pdb
Related1A1D 1DZF 1I3Q 1I50 1I6H 1K83 1NIK 1NT9 1PQV 1R5U 1R9S 1R9T 1SFO 1TWA 1TWC 1TWF 1TWG 1TWH 1WCM 1Y14 1Y1V 1Y1W 1Y1Y 1Y77 2B63 2B8K 2JA5 2JA6 2JA7 2JA8
DescriptorDNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC5, DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB11, ... (18 entities in total)
Functional Keywordstransferase, dna-directed rna polymerase, alpha-amanitin, ubl conjugation, nuclear protein, rna polymerase ii, elongation complex, mrna processing, phosphorylation, enzyme inhibition, dna damage, dna repair, zinc-finger, dna-binding, transferase/dna/rna, transcription bubble, zinc, nucleus, cytoplasm, inhibitor, magnesium, transcription inhibition, translocation intermediate, transcription, metal-binding, phosphoprotein, intermediate, fungal toxin, polymorphism, nucleotidyltransferase, transcription mechanism
Biological sourceSACCHAROMYCES CEREVISIAE (BAKERS' YEAST)
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Total number of polymer chains16
Total formula weight531503.86
Authors
Brueckner, F.,Cramer, P. (deposition date: 2008-05-27, release date: 2008-06-17, Last modification date: 2023-12-13)
Primary citationBrueckner, F.,Cramer, P.
Structural Basis of Transcription Inhibition by Alpha-Amanitin and Implications for RNA Polymerase II Translocation.
Nat.Struct.Mol.Biol., 15:811-, 2008
Cited by
PubMed Abstract: To study how RNA polymerase II translocates after nucleotide incorporation, we prepared elongation complex crystals in which pre- and post-translocation states interconvert. Crystal soaking with the inhibitor alpha-amanitin locked the elongation complex in a new state, which was refined at 3.4-A resolution and identified as a possible translocation intermediate. The DNA base entering the active site occupies a 'pretemplating' position above the central bridge helix, which is shifted and occludes the templating position. A leucine residue in the trigger loop forms a wedge at the shifted bridge helix, but moves by 13 A to close the active site during nucleotide incorporation. Our results support a Brownian ratchet mechanism that involves swinging of the trigger loop between open, wedged and closed positions, and suggest that alpha-amanitin impairs nucleotide incorporation and translocation by trapping the trigger loop and bridge helix.
PubMed: 18552824
DOI: 10.1038/NSMB.1458
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.4 Å)
Structure validation

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