Computational Structural Biology, Max Planck Institute for Biophysics, Frankfurt, Germany.
Physiology (Bethesda). 2009 Dec;24:377-86. doi: 10.1152/physiol.00030.2009.
Crystal structures of the bacterial amino acid transporter LeuT have provided the basis for understanding the conformational changes associated with substrate translocation by a multitude of transport proteins with the same fold. Biochemical and modeling studies led to a "rocking bundle" mechanism for LeuT that was validated by subsequent transporter structures. These advances suggest how coupled solute transport might be defined by the internal symmetry of proteins containing inverted structural repeats.
细菌氨基酸转运蛋白 LeuT 的晶体结构为理解与许多具有相同折叠的转运蛋白相关的底物转位的构象变化提供了基础。生化和建模研究提出了 LeuT 的“摆动束”机制,随后的转运蛋白结构验证了该机制。这些进展表明,具有反转结构重复的蛋白质的内部对称性如何定义偶联溶质转运。