1HOT
GLUCOSAMINE 6-PHOSPHATE DEAMINASE COMPLEXED WITH THE ALLOSTERIC ACTIVATOR N-ACETYL-GLUCOSAMINE-6-PHOSPHATE
1HOT の概要
エントリーDOI | 10.2210/pdb1hot/pdb |
分子名称 | GLUCOSAMINE 6-PHOSPHATE DEAMINASE, 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-glucopyranose, PHOSPHATE ION, ... (4 entities in total) |
機能のキーワード | isomerase |
由来する生物種 | Escherichia coli |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 60416.74 |
構造登録者 | Oliva, G.,Fontes, M.L.,Garratt, R.,Altamirano, M.M.,Calcagno, M.L.,Horjales, E. (登録日: 1995-11-17, 公開日: 1996-04-03, 最終更新日: 2024-02-07) |
主引用文献 | Oliva, G.,Fontes, M.R.,Garratt, R.C.,Altamirano, M.M.,Calcagno, M.L.,Horjales, E. Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution. Structure, 3:1323-1332, 1995 Cited by PubMed Abstract: Glucosamine 6-phosphate deaminase from Escherichia coli is an allosteric hexameric enzyme which catalyzes the reversible conversion of D-glucosamine 6-phosphate into D-fructose 6-phosphate and ammonium ion and is activated by N-acetyl-D-glucosamine 6-phosphate. Mechanistically, it belongs to the group of aldoseketose isomerases, but its reaction also accomplishes a simultaneous amination/deamination. The determination of the structure of this protein provides fundamental knowledge for understanding its mode of action and the nature of allosteric conformational changes that regulate its function. PubMed: 8747459DOI: 10.1016/S0969-2126(01)00270-2 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.4 Å) |
構造検証レポート
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