Structural Basis for the Selective Pb(II) Recognition of Metalloregulatory Protein PbrR691

被引:37
作者
Huang, Shanqing [1 ,2 ]
Liu, Xichun [1 ,2 ]
Wang, Dan [1 ,2 ]
Chen, Weizhong [1 ,2 ]
Hu, Qingyuan [1 ,2 ]
Wei, Tianbiao [1 ,2 ]
Zhou, Wenquan [3 ]
Gan, Jianhua [4 ]
Chen, Hao [1 ,2 ]
机构
[1] Nanjing Univ, Collaborat Innovat Ctr Chem Life Sci, Sch Chem & Chem Engn, Coordinat Chem Inst, Nanjing 210093, Jiangsu, Peoples R China
[2] Nanjing Univ, Collaborat Innovat Ctr Chem Life Sci, Sch Chem & Chem Engn, State Key Lab Coordinat Chem, Nanjing 210093, Jiangsu, Peoples R China
[3] Nanjing Univ, Sch Med, Dept Urol, Jinling Hosp, Nanjing 210093, Jiangsu, Peoples R China
[4] Fudan Univ, Sch Life Sci, Shanghai 200433, Peoples R China
基金
中国国家自然科学基金;
关键词
RALSTONIA-METALLIDURANS; LEAD(II) COORDINATION; NUCLEOTIDE-SEQUENCE; MOLECULAR-GEOMETRY; CRYSTAL-STRUCTURE; HEAVY-METALS; VSEPR MODEL; PAIR; MERR; DNA;
D O I
10.1021/acs.inorgchem.6b02397
中图分类号
O61 [无机化学];
学科分类号
070301 ; 081704 ;
摘要
The transcription regulator PbrR691, one of the MerR family proteins, shows extremely high sensitivity and selectivity toward Pb(II) in Ralstonia metallidurans CH34. Here, we present the crystal structure of PbrR691 in complex with Pb(II) at 2.0 angstrom resolution. The Pb(II) coordinates with three conserved cysteines and adopts a unique trigonal-pyramidal (hemidirected) geometry. To our knowledge, the PbrR691-Pb(II) structure provides the first three-dimensional visualization of a functional hemidirected lead(II) thiolate coordinate geometry in a protein.
引用
收藏
页码:12516 / 12519
页数:4
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