Stereochemistry of guanidine-metal interactions: Implications for L-arginine-metal interactions in protein structure and function
Stereochemistry of guanidine-metal interactions: Implications for L-arginine-metal interactions in protein structure and function
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DOI：
10.1002/prot.21127
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发表时间：
2006-11-15
影响因子：
2.9
通讯作者：
Christianson, David W.
中科院分区：
文献类型：
--
作者：
Di Costanzo, Luigi;Flores, Lloyd V., Jr.;Christianson, David W.
分析了从剑桥结构数据库中存储的晶体结构中检索到的150个胍-金属离子相互作用的几何构型。金属离子在未质子化的胍基平面上表现出较好的反配位立体化学，通常是在含二胍基团的络合物中，但偶尔也会发现单一的胍与金属的相互作用是以合成的方式进行的。在蛋白质数据库中保存的金属酶结构中发现了三种L-精氨酸-金属配位相互作用：来自大肠杆菌的生物素合成酶、His-67-&Arg人碳酸氢酶I和灭活的B.caldovelox精氨酸酶与L-精氨酸的络合物。在这些蛋白质中，L-精氨酸金属配位采用同步/平面外配位和反/平面配位立体化学。讨论了这些结果对L-精氨酸-金属相互作用在蛋白质结构和功能上的意义。尽管这种相互作用很少见，但这种分析为人们对含有L-精氨酸残基的酶的日益增长的兴趣提供了有用的参考点，这些残基具有一般碱基或金属配体的功能。
The geometries of 150 guanidine-metal ion interactions retrieved from crystal structures deposited in the Cambridge Structural Database have been analyzed. Metal ions exhibit a preference for anti coordination stereochemistry in the plane of the unprotonated guanidine group, usually in chelate complexes with a diguanidine moiety, but syn-oriented interactions are occasionally found for single guanidine-metal interactions. Three L-arginine-metal coordination interactions are found in metalloenzyme structures deposited in the Protein Data Bank: biotin synthase from E. coli, His-67 -> Arg human carbonic anhydrase I, and inactivated B. caldovelox arginase complexed with L-arginine. In these proteins, L-argininemetal coordination adopts syn/out-of-plane and anti/in-plane coordination stereochemistry. The implications of these results for L-arginine-metal interactions in protein structure and function are discussed. Although such interactions are rare, this analysis serves as a useful reference point for the growing interest in enzymes containing L-arginine residues that function as general bases or metal ligands.