4FMV
Crystal Structure Analysis of a GH30 Endoxylanase from Clostridium papyrosolvens C71
4FMV の概要
| エントリーDOI | 10.2210/pdb4fmv/pdb |
| 分子名称 | Glucuronoarabinoxylan endo-1,4-beta-xylanase (2 entities in total) |
| 機能のキーワード | alpha beta barrel, (beta/alpha)8 barrel, hydrolase |
| 由来する生物種 | Clostridium papyrosolvens |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 43939.87 |
| 構造登録者 | Bales, E.B.,Smith, J.K.,St John, F.J.,Hurlbert, J.C. (登録日: 2012-06-18, 公開日: 2013-06-19, 最終更新日: 2024-02-28) |
| 主引用文献 | St John, F.J.,Dietrich, D.,Crooks, C.,Pozharski, E.,Gonzalez, J.M.,Bales, E.,Smith, K.,Hurlbert, J.C. A novel member of glycoside hydrolase family 30 subfamily 8 with altered substrate specificity. Acta Crystallogr.,Sect.D, 70:2950-2958, 2014 Cited by PubMed Abstract: Endoxylanases classified into glycoside hydrolase family 30 subfamily 8 (GH30-8) are known to hydrolyze the hemicellulosic polysaccharide glucuronoxylan (GX) but not arabinoxylan or neutral xylooligosaccharides. This is owing to the specificity of these enzymes for the α-1,2-linked glucuronate (GA) appendage of GX. Limit hydrolysis of this substrate produces a series of aldouronates each containing a single GA substituted on the xylose penultimate to the reducing terminus. In this work, the structural and biochemical characterization of xylanase 30A from Clostridium papyrosolvens (CpXyn30A) is presented. This xylanase possesses a high degree of amino-acid identity to the canonical GH30-8 enzymes, but lacks the hallmark β8-α8 loop region which in part defines the function of this GH30 subfamily and its role in GA recognition. CpXyn30A is shown to have a similarly low activity on all xylan substrates, while hydrolysis of xylohexaose revealed a competing transglycosylation reaction. These findings are directly compared with the model GH30-8 enzyme from Bacillus subtilis, XynC. Despite its high sequence identity to the GH30-8 enzymes, CpXyn30A does not have any apparent specificity for the GA appendage. These findings confirm that the typically conserved β8-α8 loop region of these enzymes influences xylan substrate specificity but not necessarily β-1,4-xylanase function. PubMed: 25372685DOI: 10.1107/S1399004714019531 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.01 Å) |
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