| Autor: |
Andrew J. Sutherland‐Smith, Vincenzo Carbone, Linley R. Schofield, Bryan Cronin, Evert C. Duin, Ron S. Ronimus |
| Jazyk: |
angličtina |
| Rok vydání: |
2024 |
| Předmět: |
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| Zdroj: |
FEBS Open Bio, Vol 14, Iss 8, Pp 1222-1229 (2024) |
| Druh dokumentu: |
article |
| ISSN: |
2211-5463 |
| DOI: |
10.1002/2211-5463.13848 |
| Popis: |
Methyl‐coenzyme M reductase (MCR) is a multi‐subunit (α2β2γ2) enzyme responsible for methane formation via its unique F430 cofactor. The genes responsible for producing MCR (mcrA, mcrB and mcrG) are typically colocated with two other highly conserved genes mcrC and mcrD. We present here the high‐resolution crystal structure for McrD from a human gut methanogen Methanomassiliicoccus luminyensis strain B10. The structure reveals that McrD comprises a ferredoxin‐like domain assembled into an α + β barrel‐like dimer with conformational flexibility exhibited by a functional loop. The description of the M. luminyensis McrD crystal structure contributes to our understanding of this key conserved methanogen protein typically responsible for promoting MCR activity and the production of methane, a greenhouse gas. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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