Structure of human phosphopantothenoylcysteine synthetase at 2.3 Å resolution
Structure of human phosphopantothenoylcysteine synthetase at 2.3 Å resolution
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DOI：
10.1016/s0969-2126(03)00146-1
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发表时间：
2003-08-01
期刊：
影响因子：
5.7
通讯作者：
Ealick, SE
中科院分区：
文献类型：
--
作者：
Manoj, N;Strauss, E;Ealick, SE
在2.3埃分辨率下测定了人磷酸泛噻吩甲酰半胱氨酸（PPC）合成酶的结构。PPC合成酶是具有相同单体的二聚体。单体折叠的一些特征类似于一组NAD依赖性酶，而其他特征类似于核糖激酶折叠。ATP，磷酸泛酸，和半胱氨酸结合位点推导出建模研究。高度保守的ATIP结合残基包括Gly 43、Ser 61、Gly 63、Gly 66、Phe 230和Asn 258。高度保守的磷酸泛酸结合残基包括来自一个单体的Asn 59、Ala 179、Ala 180和Asp 183以及来自相邻单体的Arg 55 '。结构预测乒乓机制与最初形成的酰基腺苷酸中间体，然后释放焦磷酸和攻击;半胱氨酸形成最终产品PPC和AMP。
The structure of human phosphopantothenoylcysteine (PPC) synthetase was determined at 2.3 Angstrom resolution. PPC synthetase is a dimer with identical monomers. Some features of the monomer fold resemble a group of NAD-dependent enzymes, while other features resemble the ribokinase fold. The ATP, phosphopantothenate, and cysteine binding sites were deduced from modeling studies. Highly conserved ATIP binding residues include Gly43, Ser61, Gly63, Gly66, Phe230, and Asn258. Highly conserved phosphopantothenate binding residues include Asn59, Ala179, AIa180, and Asp183 from one monomer and Arg55' from the adjacent monomer. The structure predicts a ping pong mechanism with initial formation of an acyladenylate intermediate followed by release of pyrophosphate and attack by; cysteine to form the final products PPC and AMP.