DICP OpenIR
Cryo-EM structure of fatty acid synthase (FAS) from Rhodosporidium toruloides provides insights into the evolutionary development of fungal FAS
Fischer, Manuel1; Rhinow, Daniel2; Zhu, Zhiwei3; Mills, Deryck J.2; Zhao, Zongbao K.3,4; Vonck, Janet2; Grininger, Martin1
关键词Mega-enzyme Multifunctional Proteins Protein Assembly Acyl Carrier Protein Biofuel
刊名PROTEIN SCIENCE
2015-06-01
DOI10.1002/pro.2678
24期:6页:987-995
收录类别SCI
文章类型Article
WOS标题词Science & Technology ; Life Sciences & Biomedicine
类目[WOS]Biochemistry & Molecular Biology
研究领域[WOS]Biochemistry & Molecular Biology
关键词[WOS]ACYL-CARRIER PROTEIN ; PARTICLE ELECTRON CRYOMICROSCOPY ; MULTIENZYME COMPLEX ; RHODOTORULA-GLUTINIS ; POLYKETIDE SYNTHASES ; CRYSTAL-STRUCTURE ; YEAST ; SUBSTRATE ; RESOLUTION ; BIOSYNTHESIS
英文摘要Fungal fatty acid synthases Type I (FAS I) are up to 2.7 MDa large molecular machines composed of large multifunctional polypeptides. Half of the amino acids in fungal FAS I are involved in structural elements that are responsible for scaffolding the elaborate barrel-shaped architecture and turning fungal FAS I into highly efficient de novo producers of fatty acids. Rhodosporidium toruloides is an oleaginous fungal species and renowned for its robust conversion of carbohydrates into lipids to over 70% of its dry cell weight. Here, we use cryo-EM to determine a 7.8-angstrom reconstruction of its FAS I that reveals unexpected features; its novel form of splitting the multifunctional polypeptide chain into the two subunits and , and its duplicated ACP domains. We show that the specific distribution into and occurs by splitting at one of many possible sites that can be accepted by fungal FAS I. While, therefore, the specific distribution in and chains in R. toruloides FAS I is not correlated to increased protein activities, we also show that the duplication of ACP is an evolutionary late event and argue that duplication is beneficial for the lipid overproduction phenotype.
语种英语
WOS记录号WOS:000355151200007
引用统计
被引频次:7[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://cas-ir.dicp.ac.cn/handle/321008/146287
专题中国科学院大连化学物理研究所
作者单位1.Goethe Univ Frankfurt, Cluster Excellence Macromol Complexes, Buchmann Inst Mol Life Sci, Inst Organ Chem & Chem Biol, D-60438 Frankfurt, Germany
2.Max Planck Inst Biophys, Dept Biol Struct, D-60438 Frankfurt, Germany
3.Chinese Acad Sci, Div Biotechnol, Dalian Inst Chem Phys, Dalian 116023, Peoples R China
4.Chinese Acad Sci, Dalian Natl Lab Clean Energy, Dalian Inst Chem Phys, Dalian 116023, Peoples R China
推荐引用方式
GB/T 7714
Fischer, Manuel,Rhinow, Daniel,Zhu, Zhiwei,et al. Cryo-EM structure of fatty acid synthase (FAS) from Rhodosporidium toruloides provides insights into the evolutionary development of fungal FAS[J]. PROTEIN SCIENCE,2015,24(6):987-995.
APA Fischer, Manuel.,Rhinow, Daniel.,Zhu, Zhiwei.,Mills, Deryck J..,Zhao, Zongbao K..,...&Grininger, Martin.(2015).Cryo-EM structure of fatty acid synthase (FAS) from Rhodosporidium toruloides provides insights into the evolutionary development of fungal FAS.PROTEIN SCIENCE,24(6),987-995.
MLA Fischer, Manuel,et al."Cryo-EM structure of fatty acid synthase (FAS) from Rhodosporidium toruloides provides insights into the evolutionary development of fungal FAS".PROTEIN SCIENCE 24.6(2015):987-995.
条目包含的文件
条目无相关文件。
个性服务
推荐该条目
保存到收藏夹
查看访问统计
导出为Endnote文件
谷歌学术
谷歌学术中相似的文章
[Fischer, Manuel]的文章
[Rhinow, Daniel]的文章
[Zhu, Zhiwei]的文章
百度学术
百度学术中相似的文章
[Fischer, Manuel]的文章
[Rhinow, Daniel]的文章
[Zhu, Zhiwei]的文章
必应学术
必应学术中相似的文章
[Fischer, Manuel]的文章
[Rhinow, Daniel]的文章
[Zhu, Zhiwei]的文章
相关权益政策
暂无数据
收藏/分享
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。