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McrD binds asymmetrically to methyl-coenzyme M reductase improving active site accessibility during assembly
Open accessPreprint — published as 10.1073/pnas.2302815120
Abstract
Methyl-coenzyme M reductase (MCR) catalyzes the formation of methane and its activity accounts for nearly all biologically produced methane released into the atmosphere. The assembly of MCR is an intricate process involving the installation of a complex set of post-translational modifications and the unique Ni porphyrin cofactor F 430 . Despite decades of research, details of MCR assembly remain largely unresolved. Here, we report the structural characterization of MCR in two intermediate states of assembly. These intermediate states lack one or both F 430 cofactors and form complexes with the previously uncharacterized McrD protein. McrD is found to bind asymmetrically to MCR, displacing large regions of the alpha subunit and increasing active site accessibility for the installation of F 430 —shedding light on the assembly of MCR and the role of McrD therein. This work offers crucial information for the expression of MCR in a heterologous host and provides new targets for the design of MCR inhibitors. One-sentence summary: Structural characterization of methyl-coenzyme M reductase assembly intermediates.
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Metadata
- Authors
- Chadwick, G. L., Joiner, A. M. N., Ramesh, S., Mitchell, D. A., & Nayak, D. D.
- Affiliations
- University of California, Berkeley (US)
- University of Illinois Urbana-Champaign (US)
- Corresponding author
- Chadwick, Grayson L.
- Nayak, Dipti D.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- openRxiv
- Published
- 2023-02-03
- Volume
- 120
- Issue
- 25
- Pages
- e2302815120-e2302815120
- ISSN
- 0027-8424 (ISSN-L)
- PMC
- PMC10288656
- OpenAlex
- W4380422092
- Cited by
- 15
- References
- 1
- Citations by year
- 2026: 2 · 2025: 7 · 2024: 5 · 2023: 1
- FWCI
- 0.72
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion, cc-by-nc-nd)
- Funders
- David and Lucile Packard Foundation
- Simons Foundation
- Arnold and Mabel Beckman Foundation
- Adolph C. and Mary Sprague Miller Institute for Basic Research in Science, University of California Berkeley
- Searle Scholars Program
- Chan Zuckerberg Initiative
- Rose Hills Foundation
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM097142)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Anaerobic Digestion and Biogas Production
- Keywords
- methyl-coenzyme M reductase, coenzyme F430, enzyme assembly, active site accessibility, post-translational modification, protein-protein complex structure, heterologous expression
- MeSH terms
- Atmosphere, Hydronephrosis, Metalloporphyrins, Methane, Oxidoreductases, Ureteral Obstruction, Multicystic Dysplastic Kidney
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