Novel β-structure of YLR301w from Saccharomyces cerevisiae

Title
Novel β-structure of YLR301w from Saccharomyces cerevisiae
Authors
김국한안형준이원규이철주유명희김은경
Issue Date
2012-04
Publisher
Acta crystallographica. Section D, Biological crystallography
Citation
VOL 68, 531-540
Abstract
When the Z-type variant of human 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 -structure. It consists of an N-terminal ten-stranded -barrel with two short -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 Kd of 6.2 µM, but the biological significance of this binding requires further investigation.
URI
http://pubs.kist.re.kr/handle/201004/42312
ISSN
09074449
Appears in Collections:
KIST Publication > Article
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE