5I2D

Crystal structure of T. thermophilus TTHB099 class II transcription activation complex: TAP-RPo

Summary for 5I2D

• Entry DOI: 10.2210/pdb5i2d/pdb
• Descriptor: DNA-directed RNA polymerase subunit alpha, ZINC ION, MAGNESIUM ION, ... (11 entities in total)
• Functional Keywords: transcription, rna polymerase, catabolite activator protein, camp receptor protein, transcription-dna-rna complex, transcription/dna/rna
• Biological source: Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579); More
• Total number of polymer chains: 22
• Total formula weight: 1047019.70

Authors

Feng, Y.,Zhang, Y.,Ebright, R.H. (deposition date: 2016-02-08, release date: 2016-06-22, Last modification date: 2023-09-27)

Primary citation

Feng, Y.,Zhang, Y.,Ebright, R.H.
Structural basis of transcription activation.
Science, 352:1330-1333, 2016

PubMed Abstract: Class II transcription activators function by binding to a DNA site overlapping a core promoter and stimulating isomerization of an initial RNA polymerase (RNAP)-promoter closed complex into a catalytically competent RNAP-promoter open complex. Here, we report a 4.4 angstrom crystal structure of an intact bacterial class II transcription activation complex. The structure comprises Thermus thermophilus transcription activator protein TTHB099 (TAP) [homolog of Escherichia coli catabolite activator protein (CAP)], T. thermophilus RNAP σ(A) holoenzyme, a class II TAP-dependent promoter, and a ribotetranucleotide primer. The structure reveals the interactions between RNAP holoenzyme and DNA responsible for transcription initiation and reveals the interactions between TAP and RNAP holoenzyme responsible for transcription activation. The structure indicates that TAP stimulates isomerization through simple, adhesive, stabilizing protein-protein interactions with RNAP holoenzyme.

PubMed: 27284196
DOI: 10.1126/science.aaf4417

Experimental method

X-RAY DIFFRACTION (4.405 Å)