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CrossRef Open Access 2024 3 sitasi

The crystal structure of methanogen <scp>McrD</scp> , a methyl‐coenzyme M reductase‐associated protein

Andrew J. Sutherland‐Smith Vincenzo Carbone Linley R. Schofield Bryan Cronin Evert C. Duin +1 lainnya
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Abstrak

Methyl‐coenzyme M reductase (MCR) is a multi‐subunit (α 2 β 2 γ 2 ) enzyme responsible for methane formation via its unique F 430 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.

Penulis (6)

A

Andrew J. Sutherland‐Smith

V

Vincenzo Carbone

L

Linley R. Schofield

B

Bryan Cronin

E

Evert C. Duin

R

Ron S. Ronimus

Format Sitasi

APA MLA BibTeX
Sutherland‐Smith, A.J., Carbone, V., Schofield, L.R., Cronin, B., Duin, E.C., Ronimus, R.S. (2024). The crystal structure of methanogen <scp>McrD</scp> , a methyl‐coenzyme M reductase‐associated protein. https://doi.org/10.1002/2211-5463.13848

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Lihat di Sumber doi.org/10.1002/2211-5463.13848
Informasi Jurnal
Tahun Terbit
2024
Bahasa
en
Total Sitasi
3×
Sumber Database
CrossRef
DOI
10.1002/2211-5463.13848
Akses
Open Access ✓