التفاصيل البيبلوغرافية
| العنوان: |
The crystal structure of methanogen McrD, a methyl‐coenzyme M reductase‐associated protein |
| المؤلفون: |
Sutherland‐Smith, Andrew J., Carbone, Vincenzo, Schofield, Linley R., Cronin, Bryan, Duin, Evert C., Ronimus, Ron S. |
| المساهمون: |
Massey University, Basic Energy Sciences |
| المصدر: |
FEBS Open Bio ; ISSN 2211-5463 2211-5463 |
| بيانات النشر: |
Wiley |
| سنة النشر: |
2024 |
| المجموعة: |
Wiley Online Library (Open Access Articles via Crossref) |
| الوصف: |
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. |
| نوع الوثيقة: |
article in journal/newspaper |
| اللغة: |
English |
| DOI: |
10.1002/2211-5463.13848 |
| الإتاحة: |
https://doi.org/10.1002/2211-5463.13848Test |
| حقوق: |
http://creativecommons.org/licenses/by/4.0Test/ ; http://creativecommons.org/licenses/by/4.0Test/ |
| رقم الانضمام: |
edsbas.D0AF16B3 |
| قاعدة البيانات: |
BASE |
