Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase - A small angle X-ray scattering study in solution

	Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase - A small angle X-ray scattering study in solution
	Li, SJ; Hong XG(洪新国); Hong, XG; Shi, YY; Li, H; Wang, CC
刊名	JOURNAL OF BIOLOGICAL CHEMISTRY
	2006
卷号	281 期号:10 页码:6581-6588
通讯作者	Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China ; Chinese Acad Sci, Inst Biophys, Ctr Syst Biol, Beijing 100101, Peoples R China ; Chinese Acad Sci, Inst High Energy Phys, Beijing 100039, Peoples R China ; Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China
英文摘要	We presented for the first time a small angle x-ray scattering study of intact protein-disulfide isomerase (PDI) in solution. The restored model revealed that PDI is a short and roughly elliptical cylinder with a molecular mass of 69 kDa and dimensions of 105 x 65 x 40 angstrom, and the four thioredoxin-fold domains in the order a-b-b'-a' are arranged in an annular fashion. Atomic force microscope imaging also supported the finding that PDI appears as an approximately flat elliptical cylinder. A PDI species with apparent molecular mass of 116 kDa measured by using size-exclusion chromatography, previously assumed to be a dimer, was determined to exist mainly as a monomer by using analytical ultracentrifugation. The C-terminal fragment 441 - 491 contributed to the anomalous molecular mass determination of PDI by size-exclusion chromatography. The annular model of PDI accounted for the cooperative properties of the four domains in both the isomerase and chaperone functions of PDI.
学科主题	Biochemistry & Molecular Biology
类目[WOS]	Biochemistry & Molecular Biology
研究领域[WOS]	Biochemistry & Molecular Biology
原文出处	SCI
语种	英语
WOS记录号	WOS:000236030800054
内容类型	期刊论文
源URL	[http://ir.ihep.ac.cn/handle/311005/240084]
专题	高能物理研究所_多学科研究中心
作者单位	中国科学院高能物理研究所
推荐引用方式 GB/T 7714	Li, SJ,Hong XG,Hong, XG,et al. Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase - A small angle X-ray scattering study in solution[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2006,281(10):6581-6588.
APA	Li, SJ,洪新国,Hong, XG,Shi, YY,Li, H,&Wang, CC.(2006).Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase - A small angle X-ray scattering study in solution.JOURNAL OF BIOLOGICAL CHEMISTRY,281(10),6581-6588.
MLA	Li, SJ,et al."Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase - A small angle X-ray scattering study in solution".JOURNAL OF BIOLOGICAL CHEMISTRY 281.10(2006):6581-6588.