Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2INF

Crystal Structure of Uroporphyrinogen Decarboxylase from Bacillus subtilis

2INF の概要
エントリーDOI10.2210/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
Fan, J.,Liu, Q.,Hao, Q.,Teng, M.K.,Niu, L.W. (登録日: 2006-10-06, 公開日: 2006-10-24, 最終更新日: 2023-10-25)
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: 17122346
DOI: 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)
構造検証レポート
Validation report summary of 2inf
検証レポート(詳細版)ダウンロードをダウンロード

250059

件を2026-03-04に公開中

PDB statisticsPDBj update infoContact PDBjnumon