5AMV
Structural insights into the loss of catalytic competence in pectate lyase at low pH
5AMV の概要
| エントリーDOI | 10.2210/pdb5amv/pdb |
| 分子名称 | PECTATE LYASE, alpha-D-galactopyranuronic acid-(1-4)-alpha-D-galactopyranuronic acid-(1-4)-alpha-D-galactopyranuronic acid, CALCIUM ION, ... (6 entities in total) |
| 機能のキーワード | lyase, pectate lyase, bacillus subtillis, catalytic activity |
| 由来する生物種 | BACILLUS SUBTILIS |
| 細胞内の位置 | Secreted : P39116 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 44182.79 |
| 構造登録者 | Teixeira, S.C.M.,Ali, S.,Sondergaard, C.,Pickersgill, R. (登録日: 2015-09-02, 公開日: 2015-09-30, 最終更新日: 2024-01-10) |
| 主引用文献 | Ali, S.,Sondergaard, C.R.,Teixeira, S.,Pickersgill, R.W. Structural Insights Into the Loss of Catalytic Competence in Pectate Lyase Activity at Low Ph. FEBS Lett., 589:3242-, 2015 Cited by PubMed Abstract: Pectate lyase, a family 1 polysaccharide lyase, catalyses cleavage of the α-1,4 linkage of the polysaccharide homogalacturonan via an anti β-elimination reaction. In the Michaelis complex two calcium ions bind between the C6 carboxylate of the d-galacturonate residue and enzyme aspartates at the active centre (+1 subsite), they withdraw electrons acidifying the C5 proton facilitating its abstraction by the catalytic arginine. Here we show that activity is lost at low pH because protonation of aspartates results in the loss of the two catalytic calcium-ions causing a profound failure to correctly organise the Michaelis complex. PubMed: 26420545DOI: 10.1016/J.FEBSLET.2015.09.014 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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