3RBY

Crystal structure of uncharacterized protein YLR301w from Saccharomycces cerevisiae

Summary for 3RBY

• Entry DOI: 10.2210/pdb3rby/pdb
• Descriptor: Uncharacterized protein YLR301W, TRIETHYLENE GLYCOL, SULFATE ION, ... (4 entities in total)
• Functional Keywords: uncharacterized, beta-barrel, unknown function
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Cytoplasm : Q05905
• Total number of polymer chains: 2
• Total formula weight: 56364.67

Authors

Kim, K.-H.,Kim, E.E. (deposition date: 2011-03-30, release date: 2012-03-21, Last modification date: 2024-03-20)

Primary citation

Kim, K.H.,Ahn, H.J.,Lee, W.K.,Lee, C.,Yu, M.H.,Kim, E.E.
Novel beta-structure of YLR301w from Saccharomyces cerevisiae.
Acta Crystallogr.,Sect.D, 68:531-540, 2012

PubMed Abstract: 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.

PubMed: 22525751
DOI: 10.1107/S090744491200491X

Experimental method

X-RAY DIFFRACTION (2.301 Å)