3rby

Publication Abstract from PubMed

When the Z-type variant of human alpha(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 A resolution, revealing a novel beta-structure. It consists of an N-terminal ten-stranded beta-barrel with two short alpha-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 microM, but the biological significance of this binding requires further investigation.

Novel beta-structure of YLR301w from Saccharomyces cerevisiae.,Kim KH, Ahn HJ, Lee WK, Lee C, Yu MH, Kim EE Acta Crystallogr D Biol Crystallogr. 2012 May;68(Pt 5):531-40. Epub 2012 Apr 17. PMID:22525751^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.