Kim, Kook-Han Ahn, Hyung Jun Lee, Won-Kyu Lee, Cheolju Yu, Myeong-Hee Kim, Eunice EunKyeong 2024-01-20T15:01:17Z 2024-01-20T15:01:17Z 2021-09-05 2012-05 0907-4449 https://pubs.kist.re.kr/handle/201004/129296 When the Z-type variant of human a1-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.similar to cerevisiae YLR301w has been determined at 2.3 angstrom resolution, revealing a novel beta-structure. It consists of an N-terminal ten-stranded beta-barrel with two short a-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 similar to homodimer both in the crystal and in solution. YLR301w binds Sec72 with a Kd of 6.2 mu M, but the biological significance of this binding requires further investigation. English WILEY-BLACKWELL ACID-BINDING PROTEIN ENDOPLASMIC-RETICULUM STRESS AUTOMATED STRUCTURE SOLUTION CRYSTAL-STRUCTURE ALPHA-1-ANTITRYPSIN DEFICIENCY YEAST GENOMICS DISEASE COMPLEX KINASE Novel beta-structure of YLR301w from Saccharomyces cerevisiae Article 10.1107/S090744491200491X 1 ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, v.68, pp.531 - 540 ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 68 531 540 scie scopus 000303159000005 2-s2.0-84860290433 Biochemical Research Methods Biochemistry & Molecular Biology Biophysics Crystallography Biochemistry & Molecular Biology Biophysics Crystallography Article ACID-BINDING PROTEIN ENDOPLASMIC-RETICULUM STRESS AUTOMATED STRUCTURE SOLUTION CRYSTAL-STRUCTURE ALPHA-1-ANTITRYPSIN DEFICIENCY YEAST GENOMICS DISEASE COMPLEX KINASE YLR301w ss-barrel Z-type a1-antitrypsin sec72 Saccharomyces cerevisiae proteome analysis