3VUP

Beta-1,4-mannanase from the common sea hare Aplysia kurodai

Summary for 3VUP

• Entry DOI: 10.2210/pdb3vup/pdb
• Descriptor: Beta-1,4-mannanase, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, SULFATE ION, ... (4 entities in total)
• Functional Keywords: tim barrel, beta-1, 4-mannanase, mannan, digestive fluid, hydrolase
• Biological source: Aplysia kurodai (Kuroda's sea hare)
• Total number of polymer chains: 2
• Total formula weight: 81618.96

Authors

Mizutani, K.,Tsuchiya, S.,Toyoda, M.,Nanbu, Y.,Tominaga, K.,Yuasa, K.,Takahashi, N.,Tsuji, A.,Mikami, B. (deposition date: 2012-07-04, release date: 2012-10-17, Last modification date: 2024-10-30)

Primary citation

Mizutani, K.,Tsuchiya, S.,Toyoda, M.,Nanbu, Y.,Tominaga, K.,Yuasa, K.,Takahashi, N.,Tsuji, A.,Mikami, B.
Structure of beta-1,4-mannanase from the common sea hare Aplysia kurodai at 1.05 A resolution.
Acta Crystallogr.,Sect.F, 68:1164-1168, 2012

PubMed Abstract: β-1,4-Mannanase (EC 3.2.1.78) catalyzes the hydrolysis of β-1,4-glycosidic bonds within mannan, a major constituent group of the hemicelluloses. Bivalves and gastropods possess β-1,4-mannanase and may degrade mannan in seaweed and/or phytoplankton to obtain carbon and energy using the secreted enzymes in their digestive systems. In the present study, the crystal structure of AkMan, a gastropod β-1,4-mannanase prepared from the common sea hare Aplysia kurodai, was determined at 1.05 Å resolution. This is the first report of the three-dimensional structure of a gastropod β-1,4-mannanase. The structure was compared with bivalve β-1,4-mannanase and the roles of residues in the catalytic cleft were investigated. No obvious binding residue was found in subsite +1 and the substrate-binding site was exposed to the molecular surface, which may account for the enzymatic properties of mannanases that can digest complex substrates such as glucomannan and branched mannan.

PubMed: 23027740
DOI: 10.1107/S1744309112037074

Experimental method

X-RAY DIFFRACTION (1.05 Å)