3LPP

Crystal complex of N-terminal sucrase-isomaltase with kotalanol

3LPP の概要

• エントリーDOI: 10.2210/pdb3lpp/pdb
• 関連するPDBエントリー: 3LPO
• 分子名称: Sucrase-isomaltase, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total)
• 機能のキーワード: glycoside hydrolase family 31, isomaltase, alpha-glucosidase, cell membrane, disease mutation, disulfide bond, glycoprotein, glycosidase, hydrolase, membrane, multifunctional enzyme, polymorphism, signal-anchor, sulfation, transmembrane
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Apical cell membrane; Single-pass type II membrane protein: P14410
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 417299.67

構造登録者

Sim, L.,Rose, D.R. (登録日: 2010-02-05, 公開日: 2010-03-31, 最終更新日: 2024-10-30)

主引用文献

Sim, L.,Willemsma, C.,Mohan, S.,Naim, H.Y.,Pinto, B.M.,Rose, D.R.
Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains.
J.Biol.Chem., 285:17763-17770, 2010

PubMed Abstract: Human maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) are small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products. MGAM and SI are each composed of duplicated catalytic domains, N- and C-terminal, which display overlapping substrate specificities. The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides. Here we present the crystal structure of the human ntSI, in apo form to 3.2 A and in complex with the inhibitor kotalanol to 2.15 A resolution. Structural comparison with the previously solved structure of ntMGAM reveals key active site differences in ntSI, including a narrow hydrophobic +1 subsite, which may account for its additional substrate specificity for alpha-1,6 substrates.

PubMed: 20356844
DOI: 10.1074/jbc.M109.078980

実験手法

X-RAY DIFFRACTION (2.15 Å)