跨膜结构域
膜
生物化学
超家族
跨膜蛋白
转移酶
生物合成
基质(水族馆)
化学
脂质双层
酶
活动站点
生物物理学
立体化学
生物
基因
受体
生态学
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:2014-02-20
卷期号:343 (6173): 878-881
被引量:133
标识
DOI:10.1126/science.1246774
摘要
Catalysis in the Membrane Enzymes in the UbiA superfamily of integral membrane proteins synthesize lipid-soluble aromatics such as ubiquinones and chlorophylls that function in energy storage and energy transfer in mitochondrial and chloroplast membranes. Cheng and Li (p. 878 ) report structures of an archaeal UbiA protein in both apo and substrate-bound states. The structures show a large active site with a lateral portal that is likely to give access to the long-chain isoprenoid substrates. The findings suggest a mechanism for substrate recognition and catalysis and can explain disease-related mutants in eukaryotic homologs.
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