Snapshots of the maltose transporter during ATP hydrolysis
Snapshots of the maltose transporter during ATP hydrolysis
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DOI：
10.1073/pnas.1108858108
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发表时间：
2011-09-13
影响因子：
11.1
通讯作者：
Chen, Jue
中科院分区：
文献类型：
--
作者：
Oldham, Michael L.;Chen, Jue
ATP结合盒转运蛋白由ATP提供动力，但这些转运蛋白水解ATP的机制尚不清楚。在这项研究中，全长野生型麦芽糖转运蛋白的四种晶体结构，由腺苷5 '-（β，γ-亚氨基）三磷酸或ADP与磷酸盐类似物BeF 3-，VO 43-或AlF 4-结合稳定，被确定为2.2至2.4埃分辨率。这些结构导致在ATP水解过程中的两个酶的状态的分配，并证明在核苷酸结合结构域中的高度保守的残基的特定的功能作用，表明ATP结合盒转运蛋白催化ATP水解通过一般的基础机制。
ATP-binding cassette transporters are powered by ATP, but the mechanism by which these transporters hydrolyze ATP is unclear. In this study, four crystal structures of the full-length wild-type maltose transporter, stabilized by adenosine 5'-(beta,gamma-imido)triphosphate or ADP in conjunction with phosphate analogs BeF3-, VO43-, or AlF4-, were determined to 2.2- to 2.4-angstrom resolution. These structures led to the assignment of two enzymatic states during ATP hydrolysis and demonstrate specific functional roles of highly conserved residues in the nucleotide-binding domain, suggesting that ATP-binding cassette transporters catalyze ATP hydrolysis via a general base mechanism.