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3e3j

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3e3j, resolution 6.70Å ()
Gene: 1 (Enterobacteria phage T7)
Activity: DNA-directed RNA polymerase, with EC number 2.7.7.6
Related: 3e2e
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

Crystal Structure of an Intermediate Complex of T7 RNAP and 8nt of RNA

Publication Abstract from PubMed

Structural studies of the T7 bacteriophage DNA-dependent RNA polymerase (T7 RNAP) have shown that the conformation of the amino-terminal domain changes substantially between the initiation and elongation phases of transcription, but how this transition is achieved remains unclear. We report crystal structures of T7 RNAP bound to promoter DNA containing either a 7- or an 8-nucleotide (nt) RNA transcript that illuminate intermediate states along the transition pathway. The amino-terminal domain comprises the C-helix subdomain and the promoter binding domain (PBD), which consists of two segments separated by subdomain H. The structures of the intermediate complex reveal that the PBD and the bound promoter rotate by approximately 45 degrees upon synthesis of an 8-nt RNA transcript. This allows the promoter contacts to be maintained while the active site is expanded to accommodate a growing heteroduplex. The C-helix subdomain moves modestly toward its elongation conformation, whereas subdomain H remains in its initiation- rather than its elongation-phase location, more than 70 angstroms away.

The structure of a transcribing t7 RNA polymerase in transition from initiation to elongation., Durniak KJ, Bailey S, Steitz TA, Science. 2008 Oct 24;322(5901):553-7. PMID:18948533

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

3e3j is a 8 chain structure with sequence from Enterobacteria phage t7. Full crystallographic information is available from OCA.

See Also

Reference

  • Durniak KJ, Bailey S, Steitz TA. The structure of a transcribing t7 RNA polymerase in transition from initiation to elongation. Science. 2008 Oct 24;322(5901):553-7. PMID:18948533 doi:322/5901/553

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