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PreprintCited by 0Enzyme Structure and FunctionMetalloenzymes and iron-sulfur proteinsAdvanced Electron Microscopy Techniques and Applications

The DOI matches its Crossref record; 55 of the 55 references it cites were found in a registry or an index.

Structure of dimerized assimilatory NADPH-dependent sulfite reductase reveals the minimal interface for diflavin reductase binding

Open access
Stroupe, M. Elizabeth, Esfahani, Behrouz Ghazi, Walia, Nidhi, Neselu, Kasahun, Aragon, Mahira, Askenasy, Isabel, Wei, Hui, Mendez, Joshua·2024·Research Square
DOI 10.21203/rs.3.rs-4758050/v1

Preprint — published as 10.1038/s41467-025-58037-5 · Paper page

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Abstract

Escherichia coli NADPH-dependent assimilatory sulfite reductase (SiR) fixes sulfur for incorporation into sulfur-containing biomolecules. SiR is composed of two subunits: an NADPH, FMN, and FAD-binding diflavin reductase and an iron siroheme/Fe 4 S 4 cluster-containing oxidase. How they interact has been unknown for over 50 years because SiR is highly flexible, thus has been intransigent for traditional X-ray or cryo-EM structural analysis. A combination of the chameleon plunging system with a fluorinated lipid overcame the challenge of preserving a dimer between the subunits for high-resolution (2.84 Å) cryo-EM analysis. Here, we report the first structure of the reductase/oxidase complex, revealing how they interact in a minimal interface. Further, we determined the structural elements that discriminate between pairing a siroheme-containing oxidase with a diflavin reductase or a ferredoxin partner to channel the six electrons that reduce sulfite to sulfide.

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Metadata

Authors
Stroupe, M. E., Esfahani, B. G., Walia, N., Neselu, K., Aragon, M., Askenasy, I., Wei, H., & Mendez, J.
Affiliations
  • Florida State University (US)
  • New York Structural Biology Center (US)
  • University of Cambridge (GB)
  • Rutgers, The State University of New Jersey (US)
ORCID
Venue
Research Square
Publisher
Springer Science and Business Media LLC
Published
2024-07-29
DOI
10.21203/rs.3.rs-4758050/v1
OpenAlex
W4401158154
Cited by
0
References
55
Type
posted content
Language
en
Open access
Licence
Locations
Research Square (acceptedVersion, cc-by)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
Keywords
Escherichia coli, protein dimerization, protein-protein interfaces, sulfur fixation, electron transfer, cryo-EM structure

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