Solution structure of the N-terminal catalytic domain of human H-REV107-A novel circular permutated NlpC/P60 domain
Solution structure of the N-terminal catalytic domain of human H-REV107-A novel circular permutated NlpC/P60 domain
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DOI：
10.1016/j.febslet.2010.09.015
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发表时间：
2010-10-08
期刊：
影响因子：
3.5
通讯作者：
Xia, Bin
中科院分区：
文献类型：
--
作者：
Ren, Xiaobai;Lin, Jian;Xia, Bin
H-REV 107是一种钙离子非依赖性磷脂酶A（1/2），也是一种促凋亡蛋白，属于新的II类肿瘤抑制蛋白家族H-REV 107-like家族。在这里，我们报告的解决方案结构的N-末端催化结构域的人H-REV 107，它有一个类似的架构经典NlpC/P60域，即使他们的折叠拓扑结构是不同的，由于在初级序列中的循环排列。磷脂酶活性位点具有NlpC/P60肽酶中发现的结构保守的Cys-His-His催化三联体，表明H-REV 107对磷脂底物的催化机制应与NlpC/P60肽酶对肽的催化机制相似。由于H-REV 107与卵磷脂视黄醇酰基转移酶高度相似，我们的研究还提供了视黄醇代谢中这种必需酶的结构见解。(C)2010年欧洲生物化学学会联合会。由Elsevier B出版。V.保留所有权利。
H-REV107 is a Ca(2+)-independent phospholipase A(1/2), and it is also a pro-apoptosis protein belonging to the novel class II tumor suppressor family, H-REV107-like family. Here we report the solution structure of the N-terminal catalytic domain of human H-REV107, which has a similar architecture to classical NlpC/P60 domains, even though their fold topologies are different due to circular permutation in the primary sequence. The phospholipase active site possesses a structurally conserved Cys-His-His catalytic triad as found in NlpC/P60 peptidases, indicating H-REV107 should adopt a similar catalytic mechanism towards phospholipid substrates to that of NlpC/P60 peptidases towards peptides. As H-REV107 is highly similar to lecithin retinol acyltransferase, our study also provides structural insight to this essential enzyme in retinol metabolism. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.