The 1.6 angstrom resolution structure of activated D138L mutant of catabolite gene activator protein with two cAMP bound in each monomer

	The 1.6 angstrom resolution structure of activated D138L mutant of catabolite gene activator protein with two cAMP bound in each monomer
	Tao, WB; Gao, ZQ; Gao, ZY; Zhou, JH; Huang, ZX; Dong, YH; Yu, SN; Dong YH(董宇辉)
刊名	INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
	2011
卷号	48 期号:3 页码:459-465
关键词	Catabolite gene activator protein (CAP) Cyclic AMP (cAMP) Transcription Allostery X-ray crystallography
通讯作者	[Gao, Zengqiang ; Dong, Yuhui] Chinese Acad Sci, Inst High Energy Phys, Beijing 100049, Peoples R China ; [Tao, Wenbing ; Gao, Zhengya ; Huang, Zhongxian ; Yu, Shaoning] Fudan Univ, Dept Chem, Shanghai 200433, Peoples R China ; [Tao, Wenbing ; Gao, Zhengya ; Huang, Zhongxian ; Yu, Shaoning] Fudan Univ, Inst Biomed Sci, Shanghai 200433, Peoples R China ; [Zhou, Jiahai] Chinese Acad Sci, Inst Organ Chem, Shanghai 200032, Peoples R China
英文摘要	The X-ray crystal structure of the cAMP-liganded D138L mutant of Escherichia coil catabolite gene activator protein (CAP) was determined at a resolution of 1.66 angstrom. This high resolution crystal structure reveals four cAMP binding sites in the homodimer. Two anti conformations of cAMPs (anti-CAMP) locate between the beta-barrel and the C-helix of each subunit; two syn conformations of cAMPs (syn-cAMP) bind on the surface of the C-terminal domain. With two syn-cAMP molecules bound, the D138L CAP is highly symmetrical with both subunits assuming a "closed" conformation. These differences make the hinge region of the mutant more flexible. Protease susceptibility measurements indicate that D138L is more susceptible to proteases than that of wild type (WT) CAP. The results of protein dynamic experiments (H/D exchange measurements) indicate that the structure of D138L mutant is more dynamic than that of WT CAP, which may impact the recognition of specific DNA sequences. (C) 2011 Elsevier B.V. All rights reserved.
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:000289021400013
内容类型	期刊论文
源URL	[http://ir.ihep.ac.cn/handle/311005/237568]
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	Tao, WB,Gao, ZQ,Gao, ZY,et al. The 1.6 angstrom resolution structure of activated D138L mutant of catabolite gene activator protein with two cAMP bound in each monomer[J]. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,2011,48(3):459-465.
APA	Tao, WB.,Gao, ZQ.,Gao, ZY.,Zhou, JH.,Huang, ZX.,...&董宇辉.(2011).The 1.6 angstrom resolution structure of activated D138L mutant of catabolite gene activator protein with two cAMP bound in each monomer.INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,48(3),459-465.
MLA	Tao, WB,et al."The 1.6 angstrom resolution structure of activated D138L mutant of catabolite gene activator protein with two cAMP bound in each monomer".INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 48.3(2011):459-465.