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1XE8

Crystal structure of the YML079w protein from Saccharomyces cerevisiae reveals a new sequence family of the jelly roll fold.

1XE8 の概要
エントリーDOI10.2210/pdb1xe8/pdb
関連するPDBエントリー1XE7
分子名称Hypothetical 22.5 kDa protein in TUB1-CPR3 intergenic region, ADENINE, CITRIC ACID, ... (5 entities in total)
機能のキーワードjelly roll motif, cupin superfamily, structural genomics, yml079wp, s. cerevisiae, unknown function
由来する生物種Saccharomyces cerevisiae (baker's yeast)
タンパク質・核酸の鎖数3
化学式量合計69126.53
構造登録者
主引用文献Zhou, C.-Z.,Meyer, P.,Quevillon-Cheruel, S.,Li de La Sierra-Gallay, I.,Collinet, B.,Graille, M.,Blondeau, K.,Leulliot, N.,Sorel, I.,Poupon, A.,Janin, J.,Van Tilbeurgh, H.
Crystal structure of the YML079w protein from Saccharomyces cerevisiae reveals a new sequence family of the jelly-roll fold
Protein Sci., 14:209-215, 2005
Cited by
PubMed Abstract: We determined the three-dimensional crystal structure of the protein YML079wp, encoded by a hypothetical open reading frame from Saccharomyces cerevisiae to a resolution of 1.75 A. The protein has no close homologs and its molecular and cellular functions are unknown. The structure of the protein is a jelly-roll fold consisting of ten beta-strands organized in two parallel packed beta-sheets. The protein has strong structural resemblance to the plant storage and ligand binding proteins (canavalin, glycinin, auxin binding protein) but also to some plant and bacterial enzymes (epimerase, germin). The protein forms homodimers in the crystal, confirming measurements of its molecular mass in solution. Two monomers have their beta-sheet packed together to form the dimer. The presence of a hydrophobic ligand in a well conserved pocket inside the barrel and local sequence similarity with bacterial epimerases may suggest a biochemical function for this protein.
PubMed: 15608122
DOI: 10.1110/ps.041121305
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.8 Å)
構造検証レポート
Validation report summary of 1xe8
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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