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3GFK

Crystal structure of Bacillus subtilis Spx/RNA polymerase alpha subunit C-terminal domain complex

Summary for 3GFK
Entry DOI10.2210/pdb3gfk/pdb
DescriptorRegulatory protein spx, DNA-directed RNA polymerase subunit alpha (3 entities in total)
Functional Keywordsprotein-protein complex, cytoplasm, redox-active center, stress response, transcription, transcription regulation, dna-directed rna polymerase, nucleotidyltransferase, transferase, transcription-transferase complex, transcription/transferase
Biological sourceBacillus subtilis
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Cellular locationCytoplasm (Probable): O31602
Total number of polymer chains2
Total formula weight24670.36
Authors
Lamour, V.,Westblade, L.F.,Campbell, E.A.,Darst, S.A. (deposition date: 2009-02-27, release date: 2009-03-10, Last modification date: 2024-10-30)
Primary citationLamour, V.,Westblade, L.F.,Campbell, E.A.,Darst, S.A.
Crystal structure of the in vivo-assembled Bacillus subtilis Spx/RNA polymerase alpha subunit C-terminal domain complex
J.Struct.Biol., 168:352-356, 2009
Cited by
PubMed Abstract: The Bacillus subtilis Spx protein is a global transcription factor that interacts with the C-terminal domain of the RNA polymerase alpha subunit (alphaCTD) and regulates transcription of genes involved in thiol-oxidative stress, sporulation, competence, and organosulfur metabolism. Here we determined the X-ray crystal structure of the Spx/alphaCTD complex from an entirely new crystal form than previously reported [Newberry, K.J., Nakano, S., Zuber, P., Brennan, R.G., 2005. Crystal structure of the Bacillus subtilis anti-alpha, global transcriptional regulator, Spx, in complex with the alpha C-terminal domain of RNA polymerase. Proc. Natl. Acad. Sci. USA 102, 15839-15844]. Comparison of the previously reported sulfate-bound complex and our sulfate-free complex reveals subtle conformational changes that may be important for the role of Spx in regulating organosulfur metabolism.
PubMed: 19580872
DOI: 10.1016/j.jsb.2009.07.001
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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