Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4XLS

Crystal structure of T. aquaticus transcription initiation complex with CarD containing upstream fork promoter.

Summary for 4XLS
Entry DOI10.2210/pdb4xls/pdb
Related4XAX 4XLN 4XLP 4XLQ 4XLR
DescriptorDNA-directed RNA polymerase subunit alpha, MAGNESIUM ION, DNA-directed RNA polymerase subunit beta, ... (10 entities in total)
Functional Keywordsprotein-dna complex, bacterial transcription initiation complex, transcription
Biological sourceThermus aquaticus
More
Cellular locationCytoplasm : Q9EZJ8
Total number of polymer chains18
Total formula weight904642.72
Authors
Bae, B.,Darst, S.A. (deposition date: 2015-01-13, release date: 2015-09-23, Last modification date: 2024-10-30)
Primary citationBae, B.,Chen, J.,Davis, E.,Leon, K.,Darst, S.A.,Campbell, E.A.
CarD uses a minor groove wedge mechanism to stabilize the RNA polymerase open promoter complex.
Elife, 4:-, 2015
Cited by
PubMed Abstract: A key point to regulate gene expression is at transcription initiation, and activators play a major role. CarD, an essential activator in Mycobacterium tuberculosis, is found in many bacteria, including Thermus species, but absent in Escherichia coli. To delineate the molecular mechanism of CarD, we determined crystal structures of Thermus transcription initiation complexes containing CarD. The structures show CarD interacts with the unique DNA topology presented by the upstream double-stranded/single-stranded DNA junction of the transcription bubble. We confirm that our structures correspond to functional activation complexes, and extend our understanding of the role of a conserved CarD Trp residue that serves as a minor groove wedge, preventing collapse of the transcription bubble to stabilize the transcription initiation complex. Unlike E. coli RNAP, many bacterial RNAPs form unstable promoter complexes, explaining the need for CarD.
PubMed: 26349034
DOI: 10.7554/eLife.08505
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (4.01 Å)
Structure validation

226707

數據於2024-10-30公開中

PDB statisticsPDBj update infoContact PDBjnumon