2INF
Crystal Structure of Uroporphyrinogen Decarboxylase from Bacillus subtilis
2INF の概要
| エントリーDOI | 10.2210/pdb2inf/pdb |
| 分子名称 | Uroporphyrinogen decarboxylase (2 entities in total) |
| 機能のキーワード | (alpha-beta)8 barrel, eight parallel beta strands surrounded by eight alpha helices, lyase |
| 由来する生物種 | Bacillus subtilis |
| 細胞内の位置 | Cytoplasm : P32395 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 162025.83 |
| 構造登録者 | |
| 主引用文献 | Fan, J.,Liu, Q.,Hao, Q.,Teng, M.K.,Niu, L.W. Crystal structure of uroporphyrinogen decarboxylase from Bacillus subtilis J.Bacteriol., 189:3573-3580, 2007 Cited by PubMed Abstract: Uroporphyrinogen decarboxylase (UROD) is a branch point enzyme in the biosynthesis of the tetrapyrroles. It catalyzes the decarboxylation of four acetate groups of uroporphyrinogen III to yield coproporphyrinogen III, leading to heme and chlorophyll biosynthesis. UROD is a special type of nonoxidative decarboxylase, since no cofactor is essential for catalysis. In this work, the first crystal structure of a bacterial UROD, Bacillus subtilis UROD (UROD(Bs)), has been determined at a 2.3 A resolution. The biological unit of UROD(Bs) was determined by dynamic light scattering measurements to be a homodimer in solution. There are four molecules in the crystallographic asymmetric unit, corresponding to two homodimers. Structural comparison of UROD(Bs) with eukaryotic URODs reveals a variation of two loops, which possibly affect the binding of substrates and release of products. Structural comparison with the human UROD-coproporphyrinogen III complex discloses a similar active cleft, with five invariant polar residues (Arg29, Arg33, Asp78, Tyr154, and His322) and three invariant hydrophobic residues (Ile79, Phe144, and Phe207), in UROD(Bs). Among them, Asp78 may interact with the pyrrole NH groups of the substrate, and Arg29 is a candidate for positioning the acetate groups of the substrate. Both residues may also play catalytic roles. PubMed: 17122346DOI: 10.1128/JB.01083-06 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.3 Å) |
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