1V6X
Crystal Structure Of Xylanase From Streptomyces Olivaceoviridis E-86 Complexed With 3(3)-4-O-methyl-alpha-D-glucuronosyl-xylotriose
1V6X の概要
エントリーDOI | 10.2210/pdb1v6x/pdb |
関連するPDBエントリー | 1isx 1V6U 1V6V 1V6W 1xyf |
関連するBIRD辞書のPRD_ID | PRD_900116 PRD_900117 |
分子名称 | ENDO-1,4-BETA-D-XYLANASE, 4-O-methyl-alpha-D-glucopyranuronic acid-(1-2)-beta-D-xylopyranose-(1-4)-beta-D-xylopyranose-(1-4)-beta-D-xylopyranose, beta-D-xylopyranose-(1-4)-beta-D-xylopyranose, ... (6 entities in total) |
機能のキーワード | alpha-beta barrel, protein-sugar complex, carbohydrate binding module, hydrolase |
由来する生物種 | Streptomyces olivaceoviridis |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 96675.09 |
構造登録者 | Fujimoto, Z.,Kaneko, S.,Kuno, A.,Kobayashi, H.,Kusakabe, I.,Mizuno, H. (登録日: 2003-12-04, 公開日: 2004-04-27, 最終更新日: 2024-11-13) |
主引用文献 | Fujimoto, Z.,Kaneko, S.,Kuno, A.,Kobayashi, H.,Kusakabe, I.,Mizuno, H. Crystal structures of decorated xylooligosaccharides bound to a family 10 xylanase from Streptomyces olivaceoviridis E-86 J.Biol.Chem., 279:9606-9614, 2004 Cited by PubMed Abstract: The family 10 xylanase from Streptomyces olivaceoviridis E-86 (SoXyn10A) consists of a GH10 catalytic domain, which is joined by a Gly/Pro-rich linker to a family 13 carbohydrate-binding module (CBM13) that interacts with xylan. To understand how GH10 xylanases and CBM13 recognize decorated xylans, the crystal structure of SoXyn10A was determined in complex with alpha-l-arabinofuranosyl- and 4-O-methyl-alpha-d-glucuronosyl-xylooligosaccharides. The bound sugars were observed in the subsites of the catalytic cleft and also in subdomains alpha and gamma of CBM13. The data reveal that the binding mode of the oligosaccharides in the active site of the catalytic domain is entirely consistent with the substrate specificity and, in conjunction with the accompanying paper, demonstrate that the accommodation of the side chains in decorated xylans is conserved in GH10 xylanases of SoXyn10A against arabinoglucuronoxylan. CBM13 was shown to bind xylose or xylooligosaccharides reversibly by using nonsymmetric sugars as the ligands. The independent multiple sites in CBM13 may increase the probability of substrate binding. PubMed: 14670957DOI: 10.1074/jbc.M312293200 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.1 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード
