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TitleStructure of dimerized assimilatory NADPH-dependent sulfite reductase reveals the minimal interface for diflavin reductase binding.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 2955, Year 2025
Publish dateMar 26, 2025
AuthorsBehrouz Ghazi Esfahani / Nidhi Walia / Kasahun Neselu / Yashika Garg / Mahira Aragon / Isabel Askenasy / Hui Alex Wei / Joshua H Mendez / M Elizabeth Stroupe /
PubMed AbstractEscherichia coli NADPH-dependent assimilatory sulfite reductase (SiR) reduces sulfite by six electrons to make sulfide for incorporation into sulfur-containing biomolecules. SiR has two subunits: an ...Escherichia coli NADPH-dependent assimilatory sulfite reductase (SiR) reduces sulfite by six electrons to make sulfide for incorporation into sulfur-containing biomolecules. SiR has two subunits: an NADPH, FMN, and FAD-binding diflavin flavoprotein and a siroheme/FeS cluster-containing hemoprotein. The molecular interactions that govern subunit binding have been unknown since the discovery of SiR over 50 years ago because SiR is flexible, thus has been intransigent for traditional high-resolution structural analysis. We use a combination of the chameleon® plunging system with a fluorinated lipid to overcome the challenges of preserving a flexible molecule to determine a 2.78 Å-resolution cryo-EM structure of a minimal heterodimer complex. Chameleon®, combined with the fluorinated lipid, overcomes persistent denaturation at the air-water interface. Using a previously characterized minimal heterodimer reduces the heterogeneity of a structurally heterogeneous complex to a level that we analyze using multi-conformer cryo-EM image analysis algorithms. Here, we report the near-atomic resolution structure of the flavoprotein/hemoprotein complex, revealing how they interact in a minimal interface. Further, we determine the structural elements that discriminate between pairing a hemoprotein with a diflavin reductase, as in the E. coli homolog, or a ferredoxin partner, as in maize (Zea mays).
External linksNat Commun / PubMed:40140349 / PubMed Central
MethodsEM (single particle)
Resolution2.78 Å
Structure data

45359

9c91

EMDB-45359, PDB-9c91:
Assimilatory NADPH-dependent sulfite reductase minimal dimer
Method: EM (single particle) / Resolution: 2.78 Å

Chemicals

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

ChemComp-PO4:
PHOSPHATE ION

ChemComp-K:
Unknown entry

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-SRM:
SIROHEME

Source
  • escherichia coli (E. coli)
KeywordsFLAVOPROTEIN / sulfite reductase; hemoflavoprotein; oxidoreductase; cryo-EM

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