5xt6 | pdb_00005xt6

A sulfur-transferring catalytic intermediate of SufS-SufU complex from Bacillus subtilis

spinqualitylabelsall models 5xt6, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5xt6 is a 4 chain structure with sequence from Bacsu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PDA, ZN NonStd Res: CSS Gene: sufU, iscU, nifU, yurV, BSU32680 (BACSU), sufS, csd, yurW, BSU32690 (BACSU) Activity: Cysteine desulfurase, with EC number 2.8.1.7 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SUFU_BACSU] Its function is controversial. Has been generally assumed to be an iron-sulfur cluster assembly scaffold protein (PubMed:20097860, PubMed:21236255), but more recent evidence suggest it is a sulfurtransferase rather than a scaffold assembly protein (PubMed:24321018). Has been shown to bind low levels of a labile, air-sensitive Fe-S cluster; this can be assembled under anaerobic conditions from FeCl(3) and Li(2)S. Has been shown to be able to transfer this Fe-S cluster to an acceptor protein. Stimulates the cysteine desulfurase activity of SufS, for which it acts as a second substrate. Alkylation eliminates its ability to stimulate SufS. A mixture of SufS, SufU, Fra and L-cysteine is able to reconstitute Fe-S clusters on apo-aconitase (citB), reconstituting aconitase activity. [SUFS_BACSU] Enzyme able to deliver sulfur to partners involved in Fe-S cluster assembly. Catalyzes the removal of elemental sulfur atoms from L-cysteine to produce L-alanine. Activity is stimulated 40-to 100-fold by SufU, which acts as a second substrate for this enzyme following release of Ala, and generating SufU.S. A mixture of SufS, SufU, Fra and L-cysteine is able to reconstitute Fe-S clusters on apo-aconitase (citB), reconstituting aconitase activity. Publication Abstract from PubMed SufU is a zinc-containing protein involved in mobilization of sulfur from SufS for iron-sulfur cluster biogenesis of Bacillus subtilis. Structural basis for the sulfur transfer in SufS-SufU complex was revealed. A zinc-ligand exchange reaction upon SufS-SufU complexation provides a free thiol from Cys41 of SufU as a sulfur acceptor. Zinc-Ligand Swapping Mediated Complex Formation and Sulfur Transfer between SufS and SufU for Iron-Sulfur Cluster Biogenesis in Bacillus subtilis.,Fujishiro T, Terahata T, Kunichika K, Yokoyama N, Maruyama C, Asai K, Takahashi Y J Am Chem Soc. 2017 Dec 13. doi: 10.1021/jacs.7b11307. PMID:29235855 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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