5VI5

Structure of Mycobacterium smegmatis transcription initiation complex with a full transcription bubble

Summary for 5VI5

• Entry DOI: 10.2210/pdb5vi5/pdb
• Descriptor: DNA (49-MER), SULFATE ION, ZINC ION, ... (13 entities in total)
• Functional Keywords: dna-dependent rna polymerase, nucleotidyl transferase, transcriptioni initiation complex, transcription
• Biological source: Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155); More
• Total number of polymer chains: 10
• Total formula weight: 460526.98

Authors

Darst, S.A.,Campbell, E.A.,Lilic, M. (deposition date: 2017-04-14, release date: 2017-07-26, Last modification date: 2024-12-25)

Primary citation

Hubin, E.A.,Lilic, M.,Darst, S.A.,Campbell, E.A.
Structural insights into the mycobacteria transcription initiation complex from analysis of X-ray crystal structures.
Nat Commun, 8:16072-16072, 2017

PubMed Abstract: The mycobacteria RNA polymerase (RNAP) is a target for antimicrobials against tuberculosis, motivating structure/function studies. Here we report a 3.2 Å-resolution crystal structure of a Mycobacterium smegmatis (Msm) open promoter complex (RPo), along with structural analysis of the Msm RPo and a previously reported 2.76 Å-resolution crystal structure of an Msm transcription initiation complex with a promoter DNA fragment. We observe the interaction of the Msm RNAP α-subunit C-terminal domain (αCTD) with DNA, and we provide evidence that the αCTD may play a role in Mtb transcription regulation. Our results reveal the structure of an Actinobacteria-unique insert of the RNAP β' subunit. Finally, our analysis reveals the disposition of the N-terminal segment of Msm σ, which may comprise an intrinsically disordered protein domain unique to mycobacteria. The clade-specific features of the mycobacteria RNAP provide clues to the profound instability of mycobacteria RPo compared with E. coli.

PubMed: 28703128
DOI: 10.1038/ncomms16072

Experimental method

X-RAY DIFFRACTION (3.196 Å)