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PDBsum entry 6b6h

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Top Page protein dna_rna ligands metals Protein-protein interface(s) links
Transcription/transferase/DNA/RNA PDB id
6b6h
Contents
Protein chains
230 a.a.
1340 a.a.
1337 a.a.
79 a.a.
497 a.a.
201 a.a.
75 a.a.
DNA/RNA
Ligands
CMP ×2
Metals
_MG
_ZN ×2

References listed in PDB file
Key reference
Title Structural basis of bacterial transcription activation.
Authors B.Liu, C.Hong, R.K.Huang, Z.Yu, T.A.Steitz.
Ref. Science, 2017, 358, 947-951. [DOI no: 10.1126/science.aao1923]
PubMed id 29146813
Abstract
In bacteria, the activation of gene transcription at many promoters is simple and only involves a single activator. The cyclic adenosine 3',5'-monophosphate receptor protein (CAP), a classic activator, is able to activate transcription independently through two different mechanisms. Understanding the class I mechanism requires an intact transcription activation complex (TAC) structure at a high resolution. Here we report a high-resolution cryo-electron microscopy structure of an intactEscherichia coliclass I TAC containing a CAP dimer, a σ70-RNA polymerase (RNAP) holoenzyme, a complete class I CAP-dependent promoter DNA, and a de novo synthesized RNA oligonucleotide. The structure shows how CAP wraps the upstream DNA and how the interactions recruit RNAP. Our study provides a structural basis for understanding how activators activate transcription through the class I recruitment mechanism.
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