Liu Rujuan, Xu Hang, Wei Zhiyi, Wang Yanli, Lin Yajing, Gong Weimin
Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, People's Republic of China.
Biochem Biophys Res Commun. 2009 Jan 30;379(1):92-7. doi: 10.1016/j.bbrc.2008.12.012. Epub 2008 Dec 13.
It is well known that motion of LID and NMP-binding (NMP(bind)) domains in adenylate kinase (AK) is important in ligand binding and catalysis. However, the nature of such domain motions is poorly characterized. One of the critical hinge regions is hinge IV, which connects the CORE and LID domains. In addition, the hinge IV contains a strictly conserved residue, L171, in the AK family. To investigate the role of hinge IV, crystal structure of human adenylate kinase 4 (AK4) L171P mutant was determined. This mutation dramatically changes the orientation of the LID domain, which could be described as a novel twisted-and-closed conformation in contrast to the open and closed conformations in other AKs. This mutant provides a new example of domain motions in AK family.
众所周知，腺苷酸激酶（AK）中LID和NMP结合（NMP(bind)）结构域的运动在配体结合和催化过程中起着重要作用。然而，这种结构域运动的本质特征尚不明确。关键的铰链区域之一是铰链IV，它连接着CORE和LID结构域。此外，在AK家族中，铰链IV包含一个严格保守的残基L171。为了研究铰链IV的作用，我们测定了人腺苷酸激酶4（AK4）L171P突变体的晶体结构。该突变显著改变了LID结构域的方向，与其他AKs中的开放和闭合构象相比，可描述为一种新的扭曲闭合构象。该突变体为AK家族中结构域运动提供了一个新的例子。
