title: Crystal Structure of Bacillus subtilis Cysteine Desulfurase SufS and Its Dynamic Interaction with Frataxin and Scaffold Protein SufU.
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.
authors.affiliation: Department of Chemistry, Biochemistry, Hans-Meerwein Str. 4, Philipps University Marburg, 35043 Marburg, Germany.
authors.forename: Bastian
authors.initials: B
authors.lastname: Blauenburg
authors.affiliation: Department of Chemistry, Biochemistry, Hans-Meerwein Str. 4, Philipps University Marburg, 35043 Marburg, Germany.
authors.forename: Andreas
authors.initials: A
authors.lastname: Mielcarek
authors.affiliation: LOEWE Center for Synthetic Microbiology, Philipps University Marburg, 35043 Marburg, Germany.
authors.forename: Florian
authors.initials: F
authors.lastname: Altegoer
authors.affiliation: Department of Chemistry, Biochemistry, Hans-Meerwein Str. 4, Philipps University Marburg, 35043 Marburg, Germany.
authors.forename: Christopher D
authors.initials: CD
authors.lastname: Fage
authors.affiliation: Department of Chemistry, Biochemistry, Hans-Meerwein Str. 4, Philipps University Marburg, 35043 Marburg, Germany.
authors.forename: Uwe
authors.initials: U
authors.lastname: Linne
authors.affiliation: Department of Chemistry, Biochemistry, Hans-Meerwein Str. 4, Philipps University Marburg, 35043 Marburg, Germany.|LOEWE Center for Synthetic Microbiology, Philipps University Marburg, 35043 Marburg, Germany.
authors.forename: Gert
authors.initials: G
authors.lastname: Bange
authors.affiliation: Department of Chemistry, Biochemistry, Hans-Meerwein Str. 4, Philipps University Marburg, 35043 Marburg, Germany.
authors.forename: Mohamed A
authors.initials: MA
authors.lastname: Marahiel
mesh_terms: D000409:Alanine / Q000737:chemistry / Q000378:metabolism; D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D013437:Carbon-Sulfur Lyases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D003545:Cysteine / Q000737:chemistry / Q000378:metabolism; D041961:Deuterium Exchange Measurement / Q000379:methods; D033862:Iron-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D005810:Multigene Family; D011485:Protein Binding; D011487:Protein Conformation; D055503:Protein Multimerization; D011732:Pyridoxal Phosphate / Q000737:chemistry / Q000378:metabolism; D013440:Sulfides / Q000737:chemistry / Q000378:metabolism; D000096923:Frataxin
chemical_list: D000409:Alanine; D001426:Bacterial Proteins; D013437:Carbon-Sulfur Lyases; D003545:Cysteine; D033862:Iron-Binding Proteins; D007506:Iron-Sulfur Proteins; D011732:Pyridoxal Phosphate; D013440:Sulfides; D000096923:Frataxin; C051552:persulfides; C080546:cysteine desulfurase