4FK9

High Resolution Structure of the Catalytic Domain of Mannanase SActE_2347 from Streptomyces sp. SirexAA-E

4FK9 の概要

• エントリーDOI: 10.2210/pdb4fk9/pdb
• 分子名称: Cellulose-binding family II, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: gh5 tim barrel, glycoside hydrolase, beta-mannanase, hydrolase
• 由来する生物種: Streptomyces sp. SirexAA-E
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36470.06

構造登録者

Acheson, J.F.,Takasuka, T.E.,Fox, B.G. (登録日: 2012-06-13, 公開日: 2013-06-26, 最終更新日: 2024-02-28)

主引用文献

Takasuka, T.E.,Acheson, J.F.,Bianchetti, C.M.,Prom, B.M.,Bergeman, L.F.,Book, A.J.,Currie, C.R.,Fox, B.G.
Biochemical properties and atomic resolution structure of a proteolytically processed beta-mannanase from cellulolytic Streptomyces sp. SirexAA-E.
Plos One, 9:e94166-e94166, 2014

PubMed Abstract: β-Mannanase SACTE_2347 from cellulolytic Streptomyces sp. SirexAA-E is abundantly secreted into the culture medium during growth on cellulosic materials. The enzyme is composed of domains from the glycoside hydrolase family 5 (GH5), fibronectin type-III (Fn3), and carbohydrate binding module family 2 (CBM2). After secretion, the enzyme is proteolyzed into three different, catalytically active variants with masses of 53, 42 and 34 kDa corresponding to the intact protein, loss of the CBM2 domain, or loss of both the Fn3 and CBM2 domains. The three variants had identical N-termini starting with Ala51, and the positions of specific proteolytic reactions in the linker sequences separating the three domains were identified. To conduct biochemical and structural characterizations, the natural proteolytic variants were reproduced by cloning and heterologously expressed in Escherichia coli. Each SACTE_2347 variant hydrolyzed only β-1,4 mannosidic linkages, and also reacted with pure mannans containing partial galactosyl- and/or glucosyl substitutions. Examination of the X-ray crystal structure of the GH5 domain of SACTE_2347 suggests that two loops adjacent to the active site channel, which have differences in position and length relative to other closely related mannanases, play a role in producing the observed substrate selectivity.

PubMed: 24710170
DOI: 10.1371/journal.pone.0094166

実験手法

X-RAY DIFFRACTION (1.06 Å)