Bagautdinov Bagautdin, Matsuura Yoshinori, Bagautdinova Svetlana, Kunishima Naoki, Yutani Katsuhide
Protein Structure Analysis Team, RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 May 1;64(Pt 5):351-7. doi: 10.1107/S1744309108009846. Epub 2008 Apr 30.
The structure of human brain CutA1 (HsCutA1) has been determined using diffraction data to 2.05 A resolution. HsCutA1 has been implicated in the anchoring of acetylcholinesterase in neuronal cell membranes, while its bacterial homologue Escherichia coli CutA1 is involved in copper tolerance. Additionally, the structure of HsCutA1 bears similarity to that of the signal transduction protein PII, which is involved in regulation of nitrogen metabolism. Although several crystal structures of CutA1 from various sources with different rotation angles and degrees of interaction between trimer interfaces have been reported, the specific functional role of CutA1 is still unclear. In this study, the X-ray structure of HsCutA1 was determined in space group P2(1)2(1)2(1), with unit-cell parameters a = 68.69, b = 88.84, c = 125.33 A and six molecules per asymmetric unit. HsCutA1 is a trimeric molecule with intertwined antiparallel beta-strands; each subunit has a molecular weight of 14.6 kDa and contains 135 amino-acid residues. In order to obtain clues to the possible function of HsCutA1, its crystal structure was compared with those of other CutA1 and PII proteins.
人类大脑CutA1（HsCutA1）的结构已通过分辨率为2.05埃的衍射数据确定。HsCutA1与乙酰胆碱酯酶在神经元细胞膜中的锚定有关，而其细菌同源物大肠杆菌CutA1则参与铜耐受性。此外，HsCutA1的结构与信号转导蛋白PII的结构相似，PII参与氮代谢的调节。尽管已经报道了来自不同来源的CutA1的几种晶体结构，它们具有不同的旋转角度和三聚体界面之间的相互作用程度，但CutA1的具体功能作用仍不清楚。在本研究中，HsCutA1的X射线结构在空间群P2(1)2(1)2(1)中确定，晶胞参数为a = 68.69，b = 88.84，c = 125.33埃，每个不对称单元中有六个分子。HsCutA1是一个三聚体分子，具有相互缠绕的反平行β链；每个亚基的分子量为14.6 kDa，包含135个氨基酸残基。为了获得HsCutA1可能功能的线索，将其晶体结构与其他CutA1和PII蛋白的晶体结构进行了比较。
