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 accessPreprint — published as 10.1038/s41467-025-58037-5 · Paper page
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
- Published
- 2024-07-29
- OpenAlex
- W4401158154
- Cited by
- 0
- References
- 55
- Type
- posted content
- Language
- en
- Open access
- green
- doi.org
- 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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- CoChat. (2026). Citation check: Structure of dimerized assimilatory NADPH-dependent sulfite reductase reveals the minimal interface for diflavin reductase binding. https://app.cochat.ai/papers/10.21203/rs.3.rs-4758050/v1
- The paper
- Stroupe, M. E., Esfahani, B. G., Walia, N., Neselu, K., Aragon, M., Askenasy, I., Wei, H., & Mendez, J. (2024). Structure of dimerized assimilatory NADPH-dependent sulfite reductase reveals the minimal interface for diflavin reductase binding. Research Square. https://doi.org/10.21203/rs.3.rs-4758050/v1
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