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TitleMechanism and structural dynamics of sulfur transfer during de novo [2Fe-2S] cluster assembly on ISCU2.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 3269, Year 2024
Publish dateApr 16, 2024
AuthorsVinzent Schulz / Ralf Steinhilper / Jonathan Oltmanns / Sven-A Freibert / Nils Krapoth / Uwe Linne / Sonja Welsch / Maren H Hoock / Volker Schünemann / Bonnie J Murphy / Roland Lill /
PubMed AbstractMaturation of iron-sulfur proteins in eukaryotes is initiated in mitochondria by the core iron-sulfur cluster assembly (ISC) complex, consisting of the cysteine desulfurase sub-complex NFS1-ISD11- ...Maturation of iron-sulfur proteins in eukaryotes is initiated in mitochondria by the core iron-sulfur cluster assembly (ISC) complex, consisting of the cysteine desulfurase sub-complex NFS1-ISD11-ACP1, the scaffold protein ISCU2, the electron donor ferredoxin FDX2, and frataxin, a protein dysfunctional in Friedreich's ataxia. The core ISC complex synthesizes [2Fe-2S] clusters de novo from Fe and a persulfide (SSH) bound at conserved cluster assembly site residues. Here, we elucidate the poorly understood Fe-dependent mechanism of persulfide transfer from cysteine desulfurase NFS1 to ISCU2. High-resolution cryo-EM structures obtained from anaerobically prepared samples provide snapshots that both visualize different stages of persulfide transfer from Cys381 to Cys138 and clarify the molecular role of frataxin in optimally positioning assembly site residues for fast sulfur transfer. Biochemical analyses assign ISCU2 residues essential for sulfur transfer, and reveal that Cys138 rapidly receives the persulfide without a detectable intermediate. Mössbauer spectroscopy assessing the Fe coordination of various sulfur transfer intermediates shows a dynamic equilibrium between pre- and post-sulfur-transfer states shifted by frataxin. Collectively, our study defines crucial mechanistic stages of physiological [2Fe-2S] cluster assembly and clarifies frataxin's molecular role in this fundamental process.
External linksNat Commun / PubMed:38627381 / PubMed Central
MethodsEM (single particle)
Resolution2.41 - 2.75 Å
Structure data

EMDB-17731: Structure of the human mitochondrial iron-sulfur cluster biosynthesis complex during persulfide transfer (consensus map)
Method: EM (single particle) / Resolution: 2.41 Å

17732

8pk8

EMDB-17732, PDB-8pk8:
Structure of the human mitochondrial iron-sulfur cluster biosynthesis complex during persulfide transfer (persulfide on ISCU2)
Method: EM (single particle) / Resolution: 2.49 Å

17733

8pk9

EMDB-17733, PDB-8pk9:
Structure of the human mitochondrial iron-sulfur cluster biosynthesis complex during persulfide transfer (persulfide on NFS1 and ISCU2)
Method: EM (single particle) / Resolution: 2.58 Å

17734

8pka

EMDB-17734, PDB-8pka:
Structure of the human mitochondrial iron-sulfur cluster biosynthesis complex during persulfide transfer (without frataxin)
Method: EM (single particle) / Resolution: 2.75 Å

Chemicals

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE / Pyridoxal phosphate

ChemComp-8Q1:
S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate

ChemComp-FE2:
Unknown entry

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
  • escherichia coli bl21(de3) (bacteria)
KeywordsTRANSFERASE / cysteine desulfurase / FeS biosynthesis / FeS biogenesis / mitochondria / Friedreich's ataxia / persulfide / frataxin

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