4OOU

Crystal structure of beta-1,4-D-mannanase from Cryptopygus antarcticus

4OOU の概要

• エントリーDOI: 10.2210/pdb4oou/pdb
• 関連するPDBエントリー: 4OOZ
• 分子名称: Beta-1,4-mannanase, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total)
• 機能のキーワード: tim barrel, hydrolase
• 由来する生物種: Cryptopygus antarcticus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 85634.75

構造登録者

Kim, M.-K.,An, Y.J.,Jeong, C.-S.,Cha, S.-S. (登録日: 2014-02-04, 公開日: 2014-08-06, 最終更新日: 2024-10-30)

主引用文献

Kim, M.K.,An, Y.J.,Song, J.M.,Jeong, C.S.,Kang, M.H.,Kwon, K.K.,Lee, Y.H.,Cha, S.S.
Structure-based investigation into the functional roles of the extended loop and substrate-recognition sites in an endo-beta-1,4-d-mannanase from the Antarctic springtail, Cryptopygus antarcticus.
Proteins, 82:3217-3223, 2014

PubMed Abstract: Endo-β-1,4-D-mannanase from the Antarctic springtail, Cryptopygus antarcticus (CaMan), is a cold-adapted β-mannanase that has the lowest optimum temperature (30°C) of all known β-mannanases. Here, we report the apo- and mannopentaose (M5) complex structures of CaMan. Structural comparison of CaMan with other β-mannanases from the multicellular animals reveals that CaMan has an extended loop that alters topography of the active site. Structural and mutational analyses suggest that this extended loop is linked to the cold-adapted enzymatic activity. From the CaMan-M5 complex structure, we defined the mannose-recognition subsites and observed unreported M5 binding site on the surface of CaMan.

PubMed: 25082572
DOI: 10.1002/prot.24655

実験手法

X-RAY DIFFRACTION (2.36 Å)