4FUA
L-FUCULOSE-1-PHOSPHATE ALDOLASE COMPLEX WITH PGH
4FUA の概要
| エントリーDOI | 10.2210/pdb4fua/pdb |
| 分子名称 | L-FUCULOSE-1-PHOSPHATE ALDOLASE, ZINC ION, SULFATE ION, ... (6 entities in total) |
| 機能のキーワード | class ii aldolase, zinc enzyme, hydrolase, lyase (aldehyde) |
| 由来する生物種 | Escherichia coli |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 24215.97 |
| 構造登録者 | |
| 主引用文献 | Dreyer, M.K.,Schulz, G.E. Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure. J.Mol.Biol., 259:458-466, 1996 Cited by PubMed Abstract: The structure of L-fuculose-1-phosphate aldolase in a cubic crystal form has been determined with and without the inhibitor phosphoglycolohydroxamate at 2.4 and 2.7 angstrom (1 angstrom = 0.1 nm) resolution, respectively. This inhibitor mimics the enediolate transition state of the substrate moiety dihydroxyacetone phosphate. The structures showed that dihydroxyacetone phosphate ligates the zinc ion of this metal-dependent class II aldolase with its hydroxyl and keto oxygen atoms, shifting Glu73 away from the zinc coordination sphere to a non-polar environment. At this position Glu73 accepts a proton in the initial reaction step, producing the enediolate which is then stabilized by the zinc ion. The other substrate moiety L-lactaldehyde was modeled, because no binding structure is yet available. PubMed: 8676381DOI: 10.1006/jmbi.1996.0332 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.43 Å) |
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