ATP 结合态人 ABCF1 的晶体结构揭示 ABC 蛋白的独特构象。

Crystal Structure of ATP-Bound Human ABCF1 Demonstrates a Unique Conformation of ABC Proteins.

机构信息

Yunnan Key Laboratory of Stem Cell and Regenerative Medicine, Institute of Molecular and Clinical Medicine, Kunming Medical University, Kunming 650500, China; The Key Laboratory of Innate Immune Biology of Fujian Province, Biomedical Research Center of South China, College of Life Sciences, Fujian Normal University, Fuzhou 350117, China.

National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.

出版信息

Structure. 2018 Sep 4;26(9):1259-1265.e3. doi: 10.1016/j.str.2018.05.019. Epub 2018 Jul 12.

DOI:10.1016/j.str.2018.05.019

PMID:30017566

Abstract

Gene translation requires the correct selection of start codon AUG in mRNA. ATP-binding cassette subfamily F member 1 (ABCF1) plays a key role in the accuracy of start codon selection. However, the function of human ABCF1 is not clearly understood. Here, we solve the crystal structure of an ATP-bound wild-type human ABCF1 at 2.3-Å resolution. The comparative studies indicate that the structure is in a pre-activation intermediate conformation. This conformation is stabilized by the interaction between ATP and protein. Thus, we propose that this conformation is an important step in the activation of ABCF1. This study extends our understanding of ABC (ATP-binding cassette) protein activation at the molecular level.

摘要

基因翻译需要在 mRNA 中正确选择起始密码子 AUG。ATP 结合盒亚家族 F 成员 1（ABCF1）在起始密码子选择的准确性中发挥关键作用。然而，人类 ABCF1 的功能尚不清楚。在这里，我们解决了 2.3-Å 分辨率下结合 ATP 的野生型人 ABCF1 的晶体结构。比较研究表明，该结构处于前激活中间构象。这种构象通过 ATP 与蛋白质之间的相互作用得到稳定。因此，我们提出这种构象是 ABCF1 激活的重要步骤。本研究从分子水平扩展了我们对 ABC（ATP 结合盒）蛋白激活的理解。