6SJ9

Proteasome accessory factor B/C (PafBC) of Arthrobacter aurescens

Summary for 6SJ9

• Entry DOI: 10.2210/pdb6sj9/pdb
• Descriptor: Proteasome accessory factor B/C (PafBC), POTASSIUM ION, THIOCYANATE ION, ... (6 entities in total)
• Functional Keywords: transcriptional regulator, dna damage response, sm-fold, winged helix-turn-helix, wyl domain, ferredoxin-like fold, transcription
• Biological source: Paenarthrobacter aurescens
• Total number of polymer chains: 2
• Total formula weight: 147351.78

Authors

Mueller, A.U.,Leibundgut, M.,Ban, N.,Weber-Ban, E. (deposition date: 2019-08-13, release date: 2019-10-16, Last modification date: 2024-10-09)

Primary citation

Muller, A.U.,Leibundgut, M.,Ban, N.,Weber-Ban, E.
Structure and functional implications of WYL domain-containing bacterial DNA damage response regulator PafBC.
Nat Commun, 10:4653-4653, 2019

PubMed Abstract: In mycobacteria, transcriptional activator PafBC is responsible for upregulating the majority of genes induced by DNA damage. Understanding the mechanism of PafBC activation is impeded by a lack of structural information on this transcription factor that contains a widespread, but poorly understood WYL domain frequently encountered in bacterial transcription factors. Here, we determine the crystal structure of Arthrobacter aurescens PafBC. The protein consists of two modules, each harboring an N-terminal helix-turn-helix DNA-binding domain followed by a central WYL and a C-terminal extension (WCX) domain. The WYL domains exhibit Sm-folds, while the WCX domains adopt ferredoxin-like folds, both characteristic for RNA-binding proteins. Our results suggest a mechanism of regulation in which WYL domain-containing transcription factors may be activated by binding RNA or other nucleic acid molecules. Using an in vivo mutational screen in Mycobacterium smegmatis, we identify potential co-activator binding sites on PafBC.

PubMed: 31604936
DOI: 10.1038/s41467-019-12567-x

Experimental method

X-RAY DIFFRACTION (2.2 Å)