5J8Q

Crystal Structure of the Cysteine Desulfurase SufS of Bacillus subtilis

Summary for 5J8Q

• Entry DOI: 10.2210/pdb5j8q/pdb
• Descriptor: Cysteine desulfurase SufS, PYRIDOXAL-5'-PHOSPHATE, ALANINE, ... (4 entities in total)
• Functional Keywords: cysteine desulfurase, iron sulfur cluster, suf-system, transferase
• Biological source: Bacillus subtilis (strain 168)
• Total number of polymer chains: 1
• Total formula weight: 46316.13

Authors

Altegoer, F.,Bange, G. (deposition date: 2016-04-08, release date: 2016-07-27, Last modification date: 2024-01-10)

Primary citation

Blauenburg, B.,Mielcarek, A.,Altegoer, F.,Fage, C.D.,Linne, U.,Bange, G.,Marahiel, M.A.
Crystal Structure of Bacillus subtilis Cysteine Desulfurase SufS and Its Dynamic Interaction with Frataxin and Scaffold Protein SufU.
Plos One, 11:e0158749-e0158749, 2016

PubMed Abstract: The biosynthesis of iron sulfur (Fe-S) clusters in Bacillus subtilis is mediated by a SUF-type gene cluster, consisting of the cysteine desulfurase SufS, the scaffold protein SufU, and the putative chaperone complex SufB/SufC/SufD. Here, we present the high-resolution crystal structure of the SufS homodimer in its product-bound state (i.e., in complex with pyrodoxal-5'-phosphate, alanine, Cys361-persulfide). By performing hydrogen/deuterium exchange (H/DX) experiments, we characterized the interaction of SufS with SufU and demonstrate that SufU induces an opening of the active site pocket of SufS. Recent data indicate that frataxin could be involved in Fe-S cluster biosynthesis by facilitating iron incorporation. H/DX experiments show that frataxin indeed interacts with the SufS/SufU complex at the active site. Our findings deepen the current understanding of Fe-S cluster biosynthesis, a complex yet essential process, in the model organism B. subtilis.

PubMed: 27382962
DOI: 10.1371/journal.pone.0158749

Experimental method

X-RAY DIFFRACTION (1.702 Å)