1BE1
GLUTAMATE MUTASE (B12-BINDING SUBUNIT), NMR, MINIMIZED AVERAGE STRUCTURE
1BE1 の概要
| エントリーDOI | 10.2210/pdb1be1/pdb |
| 分子名称 | GLUTAMATE MUTASE (1 entity in total) |
| 機能のキーワード | isomerase, glutamate mutase, b12-binding subunit |
| 由来する生物種 | Clostridium tetanomorphum |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 14763.86 |
| 構造登録者 | Tollinger, M.,Konrat, R.,Hilbert, B.H.,Marsh, E.N.G.,Kraeutler, B. (登録日: 1998-05-19, 公開日: 1998-08-26, 最終更新日: 2024-05-22) |
| 主引用文献 | Tollinger, M.,Konrat, R.,Hilbert, B.H.,Marsh, E.N.,Krautler, B. How a protein prepares for B12 binding: structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum Structure, 6:1021-1033, 1998 Cited by PubMed Abstract: Glutamate mutase is an adenosylcobamide (coenzyme B12) dependent enzyme that catalyzes the reversible rearrangement of (2S)-glutamate to (2S,3S)-3-methylaspartate. The enzyme from Clostridium tetanomorphum comprises two subunits (of 53.7 and 14.8 kDa) and in its active form appears to be an alpha 2 beta 2 tetramer. The smaller subunit, termed MutS, has been characterized as the B12-binding component. Knowledge on the structure of a B12-binding apoenzyme does not exist. PubMed: 9739092DOI: 10.1016/S0969-2126(98)00103-8 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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