1K3I
Crystal Structure of the Precursor of Galactose Oxidase
1K3I の概要
| エントリーDOI | 10.2210/pdb1k3i/pdb |
| 関連するPDBエントリー | 1GOF 1GOG 1GOH |
| 分子名称 | Galactose Oxidase Precursor, alpha-D-glucopyranose, CALCIUM ION, ... (5 entities in total) |
| 機能のキーワード | 7 blade beta propeller, prosequence form, precursor of copper enzyme., oxidoreductase |
| 由来する生物種 | Fusarium sp. |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 70700.99 |
| 構造登録者 | Firbank, S.J.,Rogers, M.S.,Wilmot, C.M.,Dooley, D.M.,Halcrow, M.A.,Knowles, P.F.,McPherson, M.J.,Phillips, S.E.V. (登録日: 2001-10-03, 公開日: 2001-11-07, 最終更新日: 2024-10-30) |
| 主引用文献 | Firbank, S.J.,Rogers, M.S.,Wilmot, C.M.,Dooley, D.M.,Halcrow, M.A.,Knowles, P.F.,McPherson, M.J.,Phillips, S.E. Crystal structure of the precursor of galactose oxidase: an unusual self-processing enzyme. Proc.Natl.Acad.Sci.USA, 98:12932-12937, 2001 Cited by PubMed Abstract: Galactose oxidase (EC ) is a monomeric enzyme that contains a single copper ion and catalyses the stereospecific oxidation of primary alcohols to their corresponding aldehydes. The protein contains an unusual covalent thioether bond between a tyrosine, which acts as a radical center during the two-electron reaction, and a cysteine. The enzyme is produced in a precursor form lacking the thioether bond and also possessing an additional 17-aa pro-sequence at the N terminus. Previous work has shown that the aerobic addition of Cu(2+) to the precursor is sufficient to generate fully processed mature enzyme. The structure of the precursor protein has been determined to 1.4 A, revealing the location of the pro-sequence and identifying structural differences between the precursor and the mature protein. Structural alignment of the precursor and mature forms of galactose oxidase shows that five regions of main chain and some key residues of the active site differ significantly between the two forms. The precursor structure provides a starting point for modeling the chemistry of thioether bond formation and pro-sequence cleavage. PubMed: 11698678DOI: 10.1073/pnas.231463798 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.4 Å) |
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