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2B63

Complete RNA Polymerase II-RNA inhibitor complex

Summary for 2B63
Entry DOI10.2210/pdb2b63/pdb
Descriptor31-MER, DNA-directed RNA polymerase II subunit 9, DNA-directed RNA polymerases I/II/III subunit 10, ... (15 entities in total)
Functional Keywordsrna polymerase ii, rna, aptamer, protein-rna complex, inhibitor, transferase-rna complex, transferase/rna
Biological sourceSaccharomyces cerevisiae (baker's yeast)
More
Cellular locationNucleus: P04050 P38902 P08518 P16370 P20433 P20434 P34087 P20436 P27999
Nucleus, nucleolus: P22139 P40422
Cytoplasm: P20435
Total number of polymer chains13
Total formula weight525029.34
Authors
Kettenberger, H.,Eisenfuehr, A.,Brueckner, F.,Theis, M.,Famulok, M.,Cramer, P. (deposition date: 2005-09-30, release date: 2005-12-06, Last modification date: 2023-08-23)
Primary citationKettenberger, H.,Eisenfuehr, A.,Brueckner, F.,Theis, M.,Famulok, M.,Cramer, P.
Structure of an RNA polymerase II-RNA inhibitor complex elucidates transcription regulation by noncoding RNAs
Nat.Struct.Mol.Biol., 13:44-48, 2006
Cited by
PubMed Abstract: The noncoding RNA B2 and the RNA aptamer FC bind RNA polymerase (Pol) II and inhibit messenger RNA transcription initiation, but not elongation. We report the crystal structure of FC(*), the central part of FC RNA, bound to Pol II. FC(*) RNA forms a double stem-loop structure in the Pol II active center cleft. B2 RNA may bind similarly, as it competes with FC(*) RNA for Pol II interaction. Both RNA inhibitors apparently prevent the downstream DNA duplex and the template single strand from entering the cleft after DNA melting and thus interfere with open-complex formation. Elongation is not inhibited, as nucleic acids prebound in the cleft would exclude the RNA inhibitors. The structure also indicates that A-form RNA could interact with Pol II similarly to a B-form DNA promoter, as suggested for the bacterial transcription inhibitor 6S RNA.
PubMed: 16341226
DOI: 10.1038/nsmb1032
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.8 Å)
Structure validation

226707

数据于2024-10-30公开中

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