Hirsch A, Breed J, Saxena K, Richter O M, Ludwig B, Diederichs K, Welte W
Universität Konstanz, Fakultät für Biologie, Germany.
FEBS Lett. 1997 Mar 10;404(2-3):208-10. doi: 10.1016/s0014-5793(97)00131-2.
The crystal structure of a non-specific porin from Paracoccus denitrificans at 3.1 A resolution has been solved by molecular replacement using the porin from Rhodopseudomonas blastica as the search model. Paracoccus porin is very similar to other non-specific porins of known structure: a trimer of 16 stranded beta-barrels each with a central pore constricted by a long extracellular loop folding back against the barrel wall. The distinctive distribution of charged residues of this non-specific porin contributes to understanding the relation between structure and ion selectivity.
利用来自 Blastica 红假单胞菌的孔蛋白作为搜索模型，通过分子置换法解析了反硝化副球菌非特异性孔蛋白在 3.1 埃分辨率下的晶体结构。反硝化副球菌孔蛋白与其他已知结构的非特异性孔蛋白非常相似：由 16 股β-桶状结构组成的三聚体，每个β-桶状结构都有一个中央孔道，该孔道被一个长的细胞外环折叠回桶壁所收缩。这种非特异性孔蛋白中带电残基的独特分布有助于理解结构与离子选择性之间的关系。
