4YN3
Crystal structure of Cucumisin complex with pro-peptide
4YN3 の概要
| エントリーDOI | 10.2210/pdb4yn3/pdb |
| 分子名称 | Cucumisin, alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-L-fucopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total) |
| 機能のキーワード | subtilisin-like fold serine protease complex, hydrolase |
| 由来する生物種 | Cucumis melo (Muskmelon) 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 79042.96 |
| 構造登録者 | Murayama, K.,Kato-Murayama, M.,Yokoyama, S.,Arima, K.,Shirouzu, M. (登録日: 2015-03-09, 公開日: 2016-03-09, 最終更新日: 2024-11-06) |
| 主引用文献 | Sotokawauchi, A.,Kato-Murayama, M.,Murayama, K.,Hosaka, T.,Maeda, I.,Onjo, M.,Ohsawa, N.,Kato, D.I.,Arima, K.,Shirouzu, M. Structural basis of cucumisin protease activity regulation by its propeptide J. Biochem., 161:45-53, 2017 Cited by PubMed Abstract: Cucumisin [EC 3.4.21.25], a subtilisin-like serine endopeptidase, was isolated from melon fruit, Cucumis melo L. Mature cucumisin (67 kDa, 621 residues) is produced by removal of the propeptide (10 kDa, 88 residues) from the cucumisin precursor by subsequence processing. It is reported that cucumisin is inhibited by its own propeptide. The crystal structure of mature cucumisin is reported to be composed of three domains: the subtilisin-like catalytic domain, the protease-associated domain and the C-terminal fibronectin-III-like domain. In this study, the crystal structure of the mature cucumisin•propeptide complex was determined by the molecular replacement method and refined at 1.95 Å resolution. In this complex, the propeptide had a domain of the α-β sandwich motif with four-stranded antiparallel β-sheets, two helices and a strand of the C-terminal region. The β-sheets of the propeptide bind to two parallel surface helices of cucumisin through hydrophobic interaction and 27 hydrogen bonds. The C-terminus of the propeptide binds to the cleft of the active site as peptide substrates. The inhibitory assay suggested that the C-terminal seven residues of the propeptide do not inhibit the cucumisin activity. The crystal structure of the cucumisin•propeptide complex revealed the regulation mechanism of cucumisin activity. PubMed: 27616715DOI: 10.1093/jb/mvw053 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.95 Å) |
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