Crystal structure of a novel carboxypeptidase from the hyperthermophilic Archaeon Pyrococcus furiosus
Crystal structure of a novel carboxypeptidase from the hyperthermophilic Archaeon Pyrococcus furiosus
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DOI：
10.1016/s0969-2126(02)00698-6
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发表时间：
2002-02-01
期刊：
影响因子：
5.7
通讯作者：
Chan, MK
中科院分区：
文献类型：
--
作者：
Arndt, JW;Hao, B;Chan, MK
利用多波长异常衍射（MAD）方法测定了焦球菌羧肽酶（PfuCP）在2.2埃分辨率下的结构。PfuCP代表了新的M32羧肽酶家族的第一个结构。整体结构由同型二聚体组成。每个亚基大多是螺旋的，其最显著的特征是一个深底物结合槽。活性位点位于凹槽的底部，包含一个HEXXH基序，协调催化所需的金属离子。令人惊讶的是，这种结构与最近报道的大鼠神经溶素相似。这些结构的比较以及与其他同源蛋白的序列分析揭示了一些保守的残基。这些保守残基在催化机制中的作用是基于建模和它们的位置推断出来的。
The structure of Pyrococcus furiosus carboxypeptidase (PfuCP) has been determined to 2.2 Angstrom resolution using multiwavelength anomalous diffraction (MAD) methods. PfuCP represents the first structure of the new M32 family of carboxypeptidases. The overall structure is comprised of a homodimer. Each subunit is mostly helical with its most pronounced feature being a deep substrate binding groove. The active site lies at the bottom of this groove and contains an HEXXH motif that coordinates the metal ion required for catalysis. Surprisingly, the structure is similar to the recently reported rat neurolysin. Comparison of these structures as well as sequence analyses with other homologous proteins reveal several conserved residues. The roles for these conserved residues in the catalytic mechanism are inferred based on modeling and their location.