4E4P

Second native structure of Xylanase A1 from Paenibacillus sp. JDR-2

4E4P の概要

• エントリーDOI: 10.2210/pdb4e4p/pdb
• 関連するPDBエントリー: 3RDK 3RO8
• 分子名称: Endo-1,4-beta-xylanase A, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: xylanase, paenibacillus, tim barrel, beta/alpha 8 fold, hydrolase
• 由来する生物種: Paenibacillus sp.
• 細胞内の位置: Secreted, cell wall : C6CRV0
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 76971.74

構造登録者

Pozharski, E.,St John, F.J. (登録日: 2012-03-13, 公開日: 2012-04-18, 最終更新日: 2024-02-28)

主引用文献

St John, F.J.,Preston, J.F.,Pozharski, E.
Novel structural features of xylanase A1 from Paenibacillus sp. JDR-2.
J.Struct.Biol., 180:303-311, 2012

PubMed Abstract: The Gram-positive bacterium Paenibacillus sp. JDR-2 (PbJDR2) has been shown to have novel properties in the utilization of the abundant but chemically complex hemicellulosic sugar glucuronoxylan. Xylanase A1 of PbJDR2 (PbXynA1) has been implicated in an efficient process in which extracellular depolymerization of this polysaccharide is coupled to assimilation and intracellular metabolism. PbXynA1is a 154kDa cell wall anchored multimodular glycosyl hydrolase family 10 (GH10) xylanase. In this work, the 38kDa catalytic module of PbXynA1 has been structurally characterized revealing several new features not previously observed in structures of GH10 xylanases. These features are thought to facilitate hydrolysis of highly substituted, chemically complex xylans that may be the form found in close proximity to the cell wall of PbJDR2, an organism shown to have a preference for growth on polymeric glucuronoxylan.

PubMed: 23000703
DOI: 10.1016/j.jsb.2012.09.007

実験手法

X-RAY DIFFRACTION (1.92 Å)