دورية أكاديمية
The structure of the SufS-SufE complex reveals interactions driving protected persulfide transfer in iron-sulfur cluster biogenesis.
| العنوان: | The structure of the SufS-SufE complex reveals interactions driving protected persulfide transfer in iron-sulfur cluster biogenesis. |
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| المؤلفون: | Gogar RK; Department of Chemistry & Biochemistry, The University of Alabama, Tuscaloosa, AL, 35487, USA., Chhikara N; Department of Chemistry & Biochemistry, The University of Alabama, Tuscaloosa, AL, 35487, USA., Vo M; Department of Chemistry & Biochemistry, The University of Alabama, Tuscaloosa, AL, 35487, USA., Gilbert NC; Department of Biological Sciences, Louisiana State University, Baton Rouge, LA, 70803, USA., Dunkle JA; Department of Chemistry & Biochemistry, The University of Alabama, Tuscaloosa, AL, 35487, USA., Frantom PA; Department of Chemistry & Biochemistry, The University of Alabama, Tuscaloosa, AL, 35487, USA. |
| المصدر: | BioRxiv : the preprint server for biology [bioRxiv] 2024 May 24. Date of Electronic Publication: 2024 May 24. |
| نوع المنشور: | Journal Article; Preprint |
| اللغة: | English |
| بيانات الدورية: | Country of Publication: United States NLM ID: 101680187 Publication Model: Electronic Cited Medium: Internet ISSN: 2692-8205 (Electronic) Linking ISSN: 26928205 NLM ISO Abbreviation: bioRxiv Subsets: PubMed not MEDLINE |
| مستخلص: | Fe-S clusters are critical cofactors for redox chemistry in all organisms. The cysteine desulfurase, SufS, provides sulfur in the SUF Fe-S cluster bioassembly pathway. SufS is a dimeric, PLP-dependent enzyme that uses cysteine as a substrate to generate alanine and a covalent persulfide on an active site cysteine residue. SufS enzymes are activated by an accessory transpersulfurase protein, either SufE or SufU depending on the organism, which accepts the persulfide product and delivers it to downstream partners for Fe-S assembly. Here, using E. coli proteins, we present the first X-ray crystal structure of a SufS/SufE complex. There is a 1:1 stoichiometry with each monomeric unit of the EcSufS dimer bound to one EcSufE subunit, though one EcSufE is rotated ~7° closer to the EcSufS active site. EcSufE makes clear interactions with the α16 helix of EcSufS and site-directed mutants of several α16 residues were deficient in EcSufE binding. Analysis of the EcSufE structure showed a loss of electron density at the EcSufS/EcSufE interface for a flexible loop containing the highly conserved residue R119. An R119A EcSufE variant binds EcSufS but is not active in cysteine desulfurase assays and fails to support Fe-S cluster bioassembly in vivo. 35 S-transfer assays suggest that R119A EcSufE can receive a persulfide, suggesting the residue may function in a release mechanism. The structure of the EcSufS/EcSufE complex allows for comparison with other cysteine desulfurases to understand mechanisms of protected persulfide transfer across protein interfaces. Competing Interests: Conflict of Interest The authors declare that they have no conflicts of interest with the contents of this article. |
| التعليقات: | Update in: J Biol Chem. 2024 Aug 7:107641. doi: 10.1016/j.jbc.2024.107641. (PMID: 39122000) |
| معلومات مُعتمدة: | P30 GM124165 United States GM NIGMS NIH HHS; R01 GM112919 United States GM NIGMS NIH HHS; R35 GM142966 United States GM NIGMS NIH HHS; S10 OD021527 United States OD NIH HHS |
| فهرسة مساهمة: | Keywords: Fe-S cluster assembly pathway; cysteine desulfurase; persulfide transfer |
| تواريخ الأحداث: | Date Created: 20240603 Latest Revision: 20240813 |
| رمز التحديث: | 20240813 |
| مُعرف محوري في PubMed: | PMC11142160 |
| DOI: | 10.1101/2024.05.23.595560 |
| PMID: | 38826363 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 2692-8205 |
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| DOI: | 10.1101/2024.05.23.595560 |