Volume 27, No 4, Apr 2017

ISSN: 1001-0602 
EISSN: 1748-7838 2018 
impact factor 17.848* 
(Clarivate Analytics, 2019)

Volume 27 Issue 4, April 2017: 582-585

LETTERS TO THE EDITOR

Cryo-EM structure of Nma111p, a unique HtrA protease composed of two protease domains and four PDZ domains

Li Zhang^1,*, Xiaojing Wang^1,*, Fenghui Fan¹, Hong-Wei Wang², Jiawei Wang², Xueming Li² and Sen-Fang Sui¹

¹State Key Laboratory of Membrane Biology, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China
²Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China Correspondence: Sen-Fang Sui, E-mail: suisf@mail.tsinghua.edu.cn; Xueming Li, E-mail: lixueming@tsinghua.edu.cn; Jiawei Wang,(jwwang@tsinghua.edu.cn)

Apoptosis, a physiological form of programmed cell death, is essential for the maintenance of normal cellular homeostasis1. In the unicellular eukaryote Saccharomyces cerevisiae, a number of evolutionarily conserved apoptosis-regulatory proteins have been identified, one of which is nuclear mediator of apoptosis 111 kDa protein (Nma111p), a protease targeting Bir1p, the sole inhibitor-of-apoptosis protein (IAP) in yeast2. Nma111p is a serine protease of the HtrA family, of which a common structural feature is the presence of the trypsin-like protease domain and the post-synaptic density 95, Drosophila discs large, zona-occludens-1 (PDZ) domain3.

10.1038/cr.2017.5

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