3EXS
Crystal structure of KGPDC from Streptococcus mutans in complex with D-R5P
3EXS の概要
| エントリーDOI | 10.2210/pdb3exs/pdb |
| 関連するPDBエントリー | 3EXR 3EXT |
| 分子名称 | RmpD (Hexulose-6-phosphate synthase), RIBULOSE-5-PHOSPHATE (3 entities in total) |
| 機能のキーワード | beta barrel, lyase |
| 由来する生物種 | Streptococcus mutans |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 95861.14 |
| 構造登録者 | |
| 主引用文献 | Li, G.L.,Liu, X.,Nan, J.,Brostromer, E.,Li, L.F.,Su, X.D. Open-closed conformational change revealed by the crystal structures of 3-keto-L-gulonate 6-phosphate decarboxylase from Streptococcus mutans Biochem.Biophys.Res.Commun., 381:429-433, 2009 Cited by PubMed Abstract: The 3-keto-L-gulonate 6-phosphate decarboxylase (KGPDC) catalyses the decarboxylation of 3-keto-L-gulonate 6-phosphate to L-xylulose in the presence of magnesium ions. The enzyme is involved in L-ascorbate metabolism and plays an essential role in the pathway of glucuronate interconversion. Crystal structures of Streptococcus mutans KGPDC were determined in the absence and presence of the product analog D-ribulose 5-phosphate. We have observed an 8 A alphaB-helix movement and other structural rearrangements around the active site between the apo-structures and product analog bound structure. These drastic conformational changes upon ligand binding are the first observation of this kind for the KGPDC family. The flexibilities of both the alpha-helix lid and the side chains of Arg144 and Arg197 are associated with substrate binding and product releasing. The open-closed conformational changes of the active site, through the movements of the alpha-helix lid and the arginine residues are important for substrate binding and catalysis. PubMed: 19222992DOI: 10.1016/j.bbrc.2009.02.049 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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