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学科主题: 生命有机化学
题名: The 1.6 angstrom resolution structure of activated D138L mutant of catabolite gene activator protein with two cAMP bound in each monomer
其他题名: 降解物基因活化蛋白D38L突变体与两种cAMP的1.6埃分辨率结构报道
作者: Tao WB(陶文斌) ; Gao ZQ(高增强) ; Gao ZY(高增亚) ; Zhou JH(周佳海) ; Huang ZX(黄仲贤) ; Dong YH(董宇辉) ; Yu SN(余绍宁)
通讯作者: 董宇辉 ; 余绍宁
刊名: Int. J. Biol. Macromol.
发表日期: 2011
卷: 48, 期:3, 页:459-465
收录类别: SCI
部门归属: 中科院高能物理所; 复旦大学; 中科院上海有机化学研究所
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.
语种: 英语
相关网址: 查看原文
WOS记录号: WOS:000289021400013
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内容类型: 期刊论文
URI标识: http://ir.sioc.ac.cn/handle/331003/27831
Appears in Collections:上海有机化学研究所_期刊论文

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Recommended Citation:
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]. Int. J. Biol. Macromol.,2011,48(3):459-465.
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