Jung Heinrich
Universität Osnabrück, Fachbereich Biologie/Chemie, Abteilung Mikrobiologie, D-49069, Osnabrück, Germany.
FEBS Lett. 2002 Oct 2;529(1):73-7. doi: 10.1016/s0014-5793(02)03184-8.
Members of the sodium/substrate symporter family (SSSF, TC 2.A.21) catalyze the uptake of a wide variety of solutes including sugars, proline, pantothenate, and iodide into cells of pro- and eukaryotic origin. Extensive analyses of the topology of different SSSF proteins suggest an arrangement of 13 transmembrane domains as a common topological motif. Regions involved in sodium and/or substrate binding were identified. Furthermore, protein chemical and spectroscopic studies reveal ligand-induced structural alterations which are consistent with close interactions between the sites of sodium and substrate binding, thereby supporting an ordered binding mechanism for transport.
钠/底物同向转运体家族(SSSF,TC 2.A.21)的成员催化多种溶质进入原核和真核细胞,这些溶质包括糖类、脯氨酸、泛酸盐和碘化物。对不同SSSF蛋白拓扑结构的广泛分析表明,13个跨膜结构域的排列是一种常见的拓扑基序。已确定了参与钠和/或底物结合的区域。此外,蛋白质化学和光谱学研究揭示了配体诱导的结构改变,这与钠结合位点和底物结合位点之间的紧密相互作用一致,从而支持了一种有序的转运结合机制。