2WC7

Crystal structure of Nostoc Punctiforme Debranching Enzyme(NPDE)(Acarbose soaked)

2WC7 の概要

• エントリーDOI: 10.2210/pdb2wc7/pdb
• 関連するPDBエントリー: 2WCS 2WKG
• 分子名称: ALPHA AMYLASE, CATALYTIC REGION (2 entities in total)
• 機能のキーワード: cd/pul-hydrolyzing enzymes, hydrolase, glycosidase, neopullulanse
• 由来する生物種: NOSTOC PUNCTIFORME
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 55629.98

構造登録者

Dumbrepatil, A.-B.,Song, H.-N.,Choi, J.-H.,Park, K.-H.,Woo, E.-J. (登録日: 2009-03-10, 公開日: 2009-09-29, 最終更新日: 2023-12-13)

主引用文献

Dumbrepatil, A.-B.,Choi, J.-H.,Park, J.T.,Kim, M.J.,Kim, T.J.,Woo, E.-J.,Park, K.-H.
Structural Features of the Nostoc Punctiforme Debranching Enzyme Reveal the Basis of its Mechanism and Substrate Specificity.
Proteins, 78:348-, 2010

PubMed Abstract: The debranching enzyme Nostoc punctiforme debranching enzyme (NPDE) from the cyanobacterium Nostoc punctiforme (PCC73102) hydrolyzes the alpha-1,6 glycosidic linkages of malto-oligosaccharides. Despite its high homology to cyclodextrin/pullulan (CD/PUL)-hydrolyzing enzymes from glycosyl hydrolase 13 family (GH-13), NPDE exhibits a unique catalytic preference for longer malto-oligosaccharides (>G8), performing hydrolysis without the transgylcosylation or CD-hydrolyzing activities of other GH-13 enzymes. To investigate the molecular basis for the property of NPDE, we determined the structure of NPDE at 2.37-A resolution. NPDE lacks the typical N-terminal domain of other CD/PUL-hydrolyzing enzymes and forms an elongated dimer in a head-to-head configuration. The unique orientation of residues 25-55 in NPDE yields an extended substrate binding groove from the catalytic center to the dimeric interface. The substrate binding groove with a lengthy cavity beyond the -1 subsite exhibits a suitable architecture for binding longer malto-oligosaccharides (>G8). These structural results may provide a molecular basis for the substrate specificity and catalytic function of this cyanobacterial enzyme, distinguishing it from the classical neopullulanases and CD/PUL-hydrolyzing enzymes.

PubMed: 19768689
DOI: 10.1002/PROT.22548

実験手法

X-RAY DIFFRACTION (2.37 Å)