6TN6

X-ray structure of the endo-beta-1,4-mannanase from Thermotoga petrophila

Summary for 6TN6

• Entry DOI: 10.2210/pdb6tn6/pdb
• Related: 3PZ9
• Descriptor: Mannan endo-1,4-beta-mannosidase. Glycosyl Hydrolase family 5, SODIUM ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (11 entities in total)
• Functional Keywords: mannanase, hyperthermophile, hydrolase
• Biological source: Thermotoga petrophila RKU-1
• Total number of polymer chains: 1
• Total formula weight: 75301.65

Authors

da Silva, V.M.,Squina, F.M.,Sperenca, M.,Martin, L.,Muniz, J.R.C.,Garcia, W.,Nicolet, Y. (deposition date: 2019-12-06, release date: 2020-04-29, Last modification date: 2024-01-24)

Primary citation

da Silva, V.M.,Cabral, A.D.,Speranca, M.A.,Squina, F.M.,Muniz, J.R.C.,Martin, L.,Nicolet, Y.,Garcia, W.
High-resolution structure of a modular hyperthermostable endo-beta-1,4-mannanase from Thermotoga petrophila: The ancillary immunoglobulin-like module is a thermostabilizing domain.
Biochim Biophys Acta Proteins Proteom, 1868:140437-140437, 2020

PubMed Abstract: The endo-β-1,4-mannanase from the hyperthermostable bacterium Thermotoga petrophila (TpMan) is an enzyme that catalyzes the hydrolysis of mannan and heteromannan polysaccharides. Of the three domains that comprise TpMan, the N-terminal GH5 catalytic domain and the C-terminal carbohydrate-binding domain are connected through a central ancillary domain of unknown structure and function. In this study, we report the partial crystal structure of the TpMan at 1.45 Å resolution, so far, the first modular hyperthermostable endo-β-1,4-mannanase structure determined. The structure exhibits two domains, a (β/α)-barrel GH5 catalytic domain connected via a linker to the central domain with an immunoglobulin-like β-sandwich fold formed of seven β-strands. Functional analysis showed that whereas the immunoglobulin-like domain does not have the carbohydrate-binding function, it stacks on the GH5 catalytic domain acting as a thermostabilizing domain and allowing operation at hyperthermophilic conditions. The carbohydrate-binding domain is absent in the crystal structure most likely due to its high flexibility around the immunoglobulin-like domain which may act also as a pivot. These results represent new structural and functional information useful on biotechnological applications for biofuel and food industries.

PubMed: 32325255
DOI: 10.1016/j.bbapap.2020.140437

Experimental method

X-RAY DIFFRACTION (1.45 Å)