4D74
1.57 A crystal structure of erwinia amylovora tyrosine phosphatase amsI
4D74 の概要
エントリーDOI | 10.2210/pdb4d74/pdb |
分子名称 | PROTEIN-TYROSINE-PHOSPHATASE AMSI, SULFATE ION (3 entities in total) |
機能のキーワード | hydrolase, amylovoran, tyrosine phosphatase, phosphatase, amsi, fire blight |
由来する生物種 | ERWINIA AMYLOVORA |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 19200.89 |
構造登録者 | Benini, S.,Salomone-Stagni, M.,Caputi, L.,Cianci, M. (登録日: 2014-11-19, 公開日: 2016-01-20, 最終更新日: 2023-12-20) |
主引用文献 | Salomone-Stagni, M.,Musiani, F.,Benini, S. Characterization and 1.57 A Resolution Structure of the Key Fire Blight Phosphatase Amsi from Erwinia Amylovora Acta Crystallogr.,Sect.F, 72:903-, 2016 Cited by PubMed Abstract: AmsI is a low-molecular-weight protein tyrosine phosphatase that regulates the production of amylovoran in the Gram-negative bacterium Erwinia amylovora, a specific pathogen of rosaceous plants such as apple, pear and quince. Amylovoran is an exopolysaccharide that is necessary for successful infection. In order to shed light on AmsI, its structure was solved at 1.57 Å resolution at the same pH as its highest measured activity (pH 5.5). In the active site, a water molecule, bridging between the catalytic Arg15 and the reaction-product analogue sulfate, might be representative of the water molecule attacking the phospho-cysteine intermediate in the second step of the reaction mechanism. PubMed: 27917839DOI: 10.1107/S2053230X16018781 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.57 Å) |
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