4ZWN
Crystal Structure of a Soluble Variant of the Monoglyceride Lipase from Saccharomyces Cerevisiae
4ZWN の概要
| エントリーDOI | 10.2210/pdb4zwn/pdb |
| 分子名称 | Monoglyceride lipase, NITRATE ION, SULFATE ION, ... (5 entities in total) |
| 機能のキーワード | monoglyceride lipase, monoacylglycerol lipase, serine hydrolase, alpha/beta hydrolase, hydrolase |
| 由来する生物種 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| 細胞内の位置 | Cytoplasm: P28321 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 152437.45 |
| 構造登録者 | Aschauer, P.,Rengachari, S.,Gruber, K.,Oberer, M. (登録日: 2015-05-19, 公開日: 2016-04-27, 最終更新日: 2024-05-08) |
| 主引用文献 | Aschauer, P.,Rengachari, S.,Lichtenegger, J.,Schittmayer, M.,Das, K.M.,Mayer, N.,Breinbauer, R.,Birner-Gruenberger, R.,Gruber, C.C.,Zimmermann, R.,Gruber, K.,Oberer, M. Crystal structure of the Saccharomyces cerevisiae monoglyceride lipase Yju3p. Biochim.Biophys.Acta, 1861:462-470, 2016 Cited by PubMed Abstract: Monoglyceride lipases (MGLs) are a group of α/β-hydrolases that catalyze the hydrolysis of monoglycerides (MGs) into free fatty acids and glycerol. This reaction serves different physiological functions, namely in the last step of phospholipid and triglyceride degradation, in mammalian endocannabinoid and arachidonic acid metabolism, and in detoxification processes in microbes. Previous crystal structures of MGLs from humans and bacteria revealed conformational plasticity in the cap region of this protein and gave insight into substrate binding. In this study, we present the structure of a MGL from Saccharomyces cerevisiae called Yju3p in its free form and in complex with a covalently bound substrate analog mimicking the tetrahedral intermediate of MG hydrolysis. These structures reveal a high conservation of the overall shape of the MGL cap region and also provide evidence for conformational changes in the cap of Yju3p. The complex structure reveals that, despite the high structural similarity, Yju3p seems to have an additional opening to the substrate binding pocket at a different position compared to human and bacterial MGL. Substrate specificities towards MGs with saturated and unsaturated alkyl chains of different lengths were tested and revealed highest activity towards MG containing a C18:1 fatty acid. PubMed: 26869448DOI: 10.1016/j.bbalip.2016.02.005 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.491 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






