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4XAX

Crystal structure of Thermus thermophilus CarD in complex with the Thermus aquaticus RNA polymerase beta1 domain

Summary for 4XAX
Entry DOI10.2210/pdb4xax/pdb
DescriptorDNA-directed RNA polymerase subunit beta domain 1, CarD, 1,2-ETHANEDIOL, ... (4 entities in total)
Functional Keywordstranscription regulator
Biological sourceThermus aquaticus
More
Total number of polymer chains2
Total formula weight38425.90
Authors
Chen, J.,Bae, B.,Campbell, E.A.,Darst, S.A. (deposition date: 2014-12-15, release date: 2015-09-16, Last modification date: 2023-09-27)
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 (2.404 Å)
Structure validation

237735

数据于2025-06-18公开中

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