1OK4
Archaeal fructose 1,6-bisphosphate aldolase covalently bound to the substrate dihydroxyacetone phosphate
1OK4 の概要
エントリーDOI | 10.2210/pdb1ok4/pdb |
関連するPDBエントリー | 1OJX 1OK6 |
分子名称 | FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS I, 1,3-DIHYDROXYACETONEPHOSPHATE (3 entities in total) |
機能のキーワード | aldolase, fructose 1, 6-bisphosphate, tim barrel, glycolytic, archaeal, lyase |
由来する生物種 | THERMOPROTEUS TENAX |
タンパク質・核酸の鎖数 | 10 |
化学式量合計 | 289111.22 |
構造登録者 | Lorentzen, E.,Zwart, P.,Stark, A.,Hensel, R.,Siebers, B.,Pohl, E. (登録日: 2003-07-17, 公開日: 2003-09-04, 最終更新日: 2023-12-13) |
主引用文献 | Lorentzen, E.,Pohl, E.,Zwart, P.,Stark, A.,Russell, R.B.,Knura, T.,Hensel, R.,Siebers, B. Crystal structure of an archaeal class I aldolase and the evolution of (betaalpha)8 barrel proteins. J. Biol. Chem., 278:47253-47260, 2003 Cited by PubMed Abstract: Fructose-1,6-bisphosphate aldolase (FBPA) catalyzes the reversible cleavage of fructose 1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate in the glycolytic pathway. FBPAs from archaeal organisms have recently been identified and characterized as a divergent family of proteins. Here, we report the first crystal structure of an archaeal FBPA at 1.9-A resolution. The structure of this 280-kDa protein complex was determined using single wavelength anomalous dispersion followed by 10-fold non-crystallographic symmetry averaging and refined to an R-factor of 14.9% (Rfree 17.9%). The protein forms a dimer of pentamers, consisting of subunits adopting the ubiquitous (betaalpha)8 barrel fold. Additionally, a crystal structure of the archaeal FBPA covalently bound to dihydroxyacetone phosphate was solved at 2.1-A resolution. Comparison of the active site residues with those of classical FBPAs, which share no significant sequence identity but display the same overall fold, reveals a common ancestry between these two families of FBPAs. Structural comparisons, furthermore, establish an evolutionary link to the triosephosphate isomerases, a superfamily hitherto considered independent from the superfamily of aldolases. PubMed: 12941964DOI: 10.1074/jbc.M305922200 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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