3IHQ

Crystal Structure of Reduced C10S Spx in Complex with the Alpha C-terminal Domain of RNA Polymeras

Summary for 3IHQ

• Entry DOI: 10.2210/pdb3ihq/pdb
• Related: 1Z3E
• Descriptor: Regulatory protein spx, DNA-directed RNA polymerase subunit alpha, IMIDAZOLE, ... (4 entities in total)
• Functional Keywords: transcription regulation, oxidative stress, spx, rna polymerase, cytoplasm, disulfide bond, redox-active center, stress response, transcription, dna-directed rna polymerase, nucleotidyltransferase, transferase, transcription-transferase complex, transcription/transferase
• Biological source: Bacillus subtilis; More
• Cellular location: Cytoplasm (Probable): O31602
• Total number of polymer chains: 2
• Total formula weight: 24277.92

Authors

Newberry, K.J.,Brennan, R.G. (deposition date: 2009-07-30, release date: 2010-02-02, Last modification date: 2023-09-06)

Primary citation

Nakano, M.M.,Lin, A.,Zuber, C.S.,Newberry, K.J.,Brennan, R.G.,Zuber, P.
Promoter recognition by a complex of Spx and the C-terminal domain of the RNA polymerase alpha subunit.
Plos One, 5:e8664-e8664, 2010

PubMed Abstract: Spx, an ArsC (arsenate reductase) family member, is a global transcriptional regulator of the microbial stress response and is highly conserved amongst Gram-positive bacteria. Bacillus subtilis Spx protein exerts positive and negative control of transcription through its interaction with the C-terminal domain of the RNA polymerase (RNAP) alpha subunit (alphaCTD). Spx activates trxA (thioredoxin) and trxB (thioredoxin reductase) in response to thiol stress, and bears an N-terminal C10XXC13 redox disulfide center that is oxidized in active Spx.

PubMed: 20084284
DOI: 10.1371/journal.pone.0008664

Experimental method

X-RAY DIFFRACTION (1.9 Å)