8D8S

SufS from Staphylococcus aureus

Summary for 8D8S

• Entry DOI: 10.2210/pdb8d8s/pdb
• Descriptor: Cysteine desulfurase, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: sufs, cysteine desulfurase, iron-sulfur cluster biosynthesis, biosynthetic protein
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 1
• Total formula weight: 46689.45

Authors

Morrison, C.N.,Boncella, A.E.,Lunin, V. (deposition date: 2022-06-08, release date: 2022-12-07, Last modification date: 2023-11-15)

Primary citation

Hudspeth, J.D.,Boncella, A.E.,Sabo, E.T.,Andrews, T.,Boyd, J.M.,Morrison, C.N.
Structural and Biochemical Characterization of Staphylococcus aureus Cysteine Desulfurase Complex SufSU.
Acs Omega, 7:44124-44133, 2022

PubMed Abstract: In this work, we provide the first in vitro characterization of two essential proteins from (. ) involved in iron-sulfur (Fe-S) cluster biogenesis: the cysteine desulfurase SufS and the sulfurtransferase SufU. Together, these proteins form the transient SufSU complex and execute the first stage of Fe-S cluster biogenesis in the SUF-like pathway in Gram-positive bacteria. The proteins involved in the SUF-like pathway, such as SufS and SufU, are essential in Gram-positive bacteria since these bacteria tend to lack redundant Fe-S cluster biogenesis pathways. Most previous work characterizing the SUF-like pathway has focused on (. ). We focus on the SUF-like pathway in because of its potential to serve as a therapeutic target to treat infections. Herein, we characterize SufS (SufS) by X-ray crystallography and UV-vis spectroscopy, and we characterize SufU (SufU) by a zinc binding fluorescence assay and small-angle X-ray scattering. We show that SufS is a type II cysteine desulfurase and that SufU is a Zn-containing sulfurtransferase. Additionally, we evaluated the cysteine desulfurase activity of the SufSU complex and compared its activity to that of SufSU. Subsequent cross-species activity analysis reveals a surprising result: SufS is significantly less stimulated by SufU than SufS. Our results set a basis for further characterization of SufSU as well as the development of new therapeutic strategies for treating infections caused by by inhibiting the SUF-like pathway.

PubMed: 36506149
DOI: 10.1021/acsomega.2c05576

Experimental method

X-RAY DIFFRACTION (1.388 Å)