Kim Kook-Han, Ahn Hyung Jun, Lee Won-Kyu, Lee Cheolju, Yu Myeong-Hee, Kim Eunice EunKyeong
Biomedical Research Institute, Korea Institute of Science and Technology, 39-1 Hawolkok-dong, Sungbuk-gu, Seoul 136-791, Republic of Korea.
Acta Crystallogr D Biol Crystallogr. 2012 May;68(Pt 5):531-40. doi: 10.1107/S090744491200491X. Epub 2012 Apr 17.
When the Z-type variant of human α(1)-antitrypsin was overexpressed in Saccharomyces cerevisiae, proteomics analysis identified YLR301w as one of the up-regulated proteins. YLR301w is a 27.5 kDa protein with no sequence homology to any known protein and has been reported to interact with Sec72 and Hrr25. The crystal structure of S. cerevisiae YLR301w has been determined at 2.3 Å resolution, revealing a novel β-structure. It consists of an N-terminal ten-stranded β-barrel with two short α-helices connected by a 23-residue linker to a seven-stranded half-barrel with two short helices at the C-terminus. The N-terminal barrel has a highly conserved hydrophobic channel that can bind hydrophobic molecules such as PEG. It forms a homodimer both in the crystal and in solution. YLR301w binds Sec72 with a K(d) of 6.2 µM, but the biological significance of this binding requires further investigation.
当人α(1)-抗胰蛋白酶的Z型变体在酿酒酵母中过表达时，蛋白质组学分析确定YLR301w是上调的蛋白质之一。YLR301w是一种27.5 kDa的蛋白质，与任何已知蛋白质均无序列同源性，据报道它与Sec72和Hrr25相互作用。酿酒酵母YLR301w的晶体结构已在2.3 Å分辨率下确定，揭示了一种新型β结构。它由一个N端十链β桶组成，有两个短α螺旋通过一个23个残基的连接子与一个七链半桶相连，在C端有两个短螺旋。N端桶有一个高度保守的疏水通道，可以结合疏水分子如聚乙二醇。它在晶体和溶液中均形成同二聚体。YLR301w以6.2 µM的解离常数结合Sec72，但这种结合的生物学意义需要进一步研究。
