Metalloenzymes and signal transduction: The protein serine/threonine phosphatases, a novel class of binuclear metal-containing enzymes

被引:38
作者
Rusnak, F [1 ]
Yu, LA [1 ]
Mertz, P [1 ]
机构
[1] MAYO CLIN & MAYO FDN,DEPT BIOCHEM & MOL BIOL,ROCHESTER,MN 55905
来源
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY | 1996年 / 1卷 / 05期
关键词
iron; protein phosphatase; metalloenzyme; calmodulin; phosphoesterase;
D O I
10.1007/s007750050070
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The serine/threonine protein phosphatases are important regulatory enzymes involved in signal transduction pathways in eukaryotic organisms. These enzymes include protein phosphatases 1, 2A, and 2B (also known as calcineurin). Recent structural data have indicated that the serine/threonine protein phosphatases are novel metalloenzymes containing a dinuclear metal ion cofactor at the active site. The dinuclear metal site is situated in a unique protein fold, a beta-alpha-beta-alpha-beta motif which provides the majority of Ligands to the metal ions. A similar fold is also seen in plant purple acid phosphatases, which also contain a dinuclear iron-zinc cofactor. In these enzymes, the two metal ions are bridged by a solvent molecule and a carboxylate group from an aspartic acid residue, juxtaposing the two metal ions to within 3.0-4.0 Angstrom of each other. A similar motif has been identified in a number of other enzymes which exhibit phosphoesterase activity, implicating several of them as metalloenzymes which contain dinuclear metal ion cofactors.
引用
收藏
页码:388 / 396
页数:9
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