1MVE

Crystal structure of a natural circularly-permutated jellyroll protein: 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes

Summary for 1MVE

• Entry DOI: 10.2210/pdb1mve/pdb
• Descriptor: Truncated 1,3-1,4-beta-D-glucanase, CALCIUM ION (3 entities in total)
• Functional Keywords: circular-permutated jellyroll protein, hydrolase
• Biological source: Fibrobacter succinogenes
• Total number of polymer chains: 1
• Total formula weight: 27405.44

Authors

Tsai, L.-C.,Shyur, L.-F.,Lee, S.-H.,Lin, S.-S.,Yuan, H.S. (deposition date: 2002-09-25, release date: 2003-07-15, Last modification date: 2022-12-21)

Primary citation

Tsai, L.C.,Shyur, L.F.,Lee, S.H.,Lin, S.S.,Yuan, H.S.
Crystal Structure of a Natural Circularly Permuted Jellyroll Protein: 1,3-1,4-beta-D-Glucanase from Fibrobacter succinogenes.
J.Mol.Biol., 330:607-620, 2003

PubMed Abstract: The 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes (Fsbeta-glucanase) is classified as one of the family 16 glycosyl hydrolases. It hydrolyzes the glycosidic bond in the mixed-linked glucans containing beta-1,3- and beta-1,4-glycosidic linkages. We constructed a truncated form of recombinant Fsbeta-glucanase containing the catalytic domain from amino acid residues 1-258, which exhibited a higher thermal stability and enzymatic activity than the full-length enzyme. The crystal structure of the truncated Fsbeta-glucanase was solved at a resolution of 1.7A by the multiple wavelength anomalous dispersion (MAD) method using the anomalous signals from the seleno-methionine-labeled protein. The overall topology of the truncated Fsbeta-glucanase consists mainly of two eight-stranded anti-parallel beta-sheets arranged in a jellyroll beta-sandwich, similar to the fold of many glycosyl hydrolases and carbohydrate-binding modules. Sequence comparison with other bacterial glucanases showed that Fsbeta-glucanase is the only naturally occurring circularly permuted beta-glucanase with reversed sequences. Structural comparison shows that the engineered circular-permuted Bacillus enzymes are more similar to their parent enzymes with which they share approximately 70% sequence identity, than to the naturally occurring Fsbeta-glucanase of similar topology with 30% identity. This result suggests that protein structure relies more on sequence identity than topology. The high-resolution structure of Fsbeta-glucanase provides a structural rationale for the different activities obtained from a series of mutant glucanases and a basis for the development of engineered enzymes with increased activity and structural stability.

PubMed: 12842475
DOI: 10.1016/S0022-2836(03)00630-2

Experimental method

X-RAY DIFFRACTION (1.7 Å)