Refined crystal structure of calcium-liganded carp parvalbumin 4.25 at 1.5-A resolution.
Refined crystal structure of calcium-liganded carp parvalbumin 4.25 at 1.5-A resolution.
复制标题
钙配体鲤鱼小清蛋白 4.25 的精细晶体结构，分辨率为 1.5-A。
DOI：
10.1021/bi00458a010
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发表时间：
1990
期刊：
影响因子：
2.9
通讯作者：
Edwards,BF
中科院分区：
文献类型：
--
作者：
Kumar,VD;Lee,L;Edwards,BF
生物化学系，韦恩州立大学医学院，底特律，密歇根州48201，和化学和生物化学系，温莎大学，温莎，加拿大N9 B 3 P4接收日期：1989年6月6日;修订版Mandarin pt接收日期：1989年10月9日摘要：本文用X射线衍射仪数据对鲤鱼小清蛋白（pi= 4.25）的晶体结构进行了最小二乘修正，使其分辨率达到1.5埃。在10和1.5 μ m之间的12653次反射的最终残差为0.215，其中I（hkl）> 2（）。在最小二乘分析中总共包括74个溶剂分子。与理想键长的均方根偏差为0.024 Ω。该模型与先前报道的结构中主链原子位置的均方根差为0.59 μ m [Moews，P.C.，& Kretsinger，R. H.等（1975）J. Mol. 91，201-228]，其使用通过膜收集的数据通过差傅立叶合成精制至1.9 μ m。虽然两种模型的总体特征非常相似，但在氨基末端区域（被广泛地重新装配）以及在CD和EF位点上与钙配位的氧原子数量（CD位点从6个增加到7个，EF位点从8个减少到7个）方面存在显著差异。主要存在于脊椎动物肌肉组织中的钙结合蛋白。它们的性质包括酸性等电点、富含苯丙氨酸和丙氨酸的氨基酸组成，以及2摩尔钙/摩尔蛋白质的结合位点，解离常数为10 - 7- 1CT 9 M [Kretsinger（1980）中综述]。钙结合小清蛋白首先由Deuticke（1934）在青蛙肌肉中发现，并由Hamoir（1951）进一步鉴定。小清蛋白现已从多种鱼类如鲤鱼的肌肉中分离出来（Konusu等人，1965）、无须鳕（Pechére等，1971）、梭子鱼（Rao & Germinal，1973）和其他脊椎动物如青蛙（Pechéreet al.，1973）和鸡肉（Heizmann & Strehler，1979）。最近还在大鼠大脑皮层的含-氨基丁酸的细胞中鉴定出小清蛋白（Celio，1986）。除了鲤鱼4.25小清蛋白之外，已经确定了Opsanus tau小清蛋白的晶体结构（Kahn等人，1985）和pike 4.1小清蛋白（Declercq等，1988年）。
Department of Biochemistry, Wayne StateUniversity School of Medicine, Detroit, Michigan 48201, and Department of Chemistry and Biochemistry, University of Windsor, Windsor, Canada N9B 3P4 Received June 6, 1989; Revised Manuscript Received October 9, 1989 abstract: Thecrystal structure of carp parvalbumin (pi= 4.25) has been refined by restrained least-squares analysis employing X-ray diffractometer data to 1.5-A resolution. The final residual for 12653 reflections between 10 and 1.5 Á with I (hkl)> 2 () is 0.215. A total of 74 solvent molecules were included in the least-squares analysis. The root mean square deviation from ideality of bond lengths is 0.024 Á. Themodel has a root mean square differenceof 0.59 Á from the positions of the main-chain atoms in a previously reported structure [Moews, P. C., & Kretsinger, R. H.(1975) J. Mol. Biol. 91, 201-228], which was refined by difference Fourier syntheses using data collected by film to 1.9 Á. Although the overall features of the two models are very similar, there are significant differencesin the amino-terminal region, which was extensively refit, and in the numberof oxygen atoms liganding calcium in the CD and EF sites, which increased from six to seven in the CD site and decreased from eight to seven in the EF site.I^ rvalbumins are small, calcium-binding proteins that are found primarily in the muscle tissue of vertebrates. Their properties include acidic isoelectric points, amino acid com-positions rich in phenylalanine and alanine, and binding sites for 2 mol of calcium/mol of protein with dissociation constants of 10 “7-1CT9 M [reviewed in Kretsinger (1980)]. Calciumbinding parvalbumin was first identified in frog muscle by Deuticke (1934) and further characterizedby Hamoir (1951). Parvalbumins have now been isolated from the muscles of a wide variety of fish such as carp (Konusu et al., 1965), hake (Pechére et al., 1971), pike (Rao & Geraday, 1973), and other vertebrates such as frog (Pechéreet al., 1973) and chicken (Heizmann & Strehler, 1979). A parvalbumin has also re-cently been identified in the-aminobutyric acid containing cells of the rat cerebral cortex (Celio, 1986). Besides carp 4.25 parvalbumin, crystal structures have been reportedfor Opsanus tau parvalbumin (Kahn et al., 1985) and pike 4.1 parvalbumin (Declercq et al., 1988).