Unknown

Dataset Information

0

Three-dimensional structure of (1,4)-beta-D-mannan mannanohydrolase from tomato fruit.


ABSTRACT: The three-dimensional crystal structure of tomato (Lycopersicon esculentum) beta-mannanase 4a (LeMAN4a) has been determined to 1.5 A resolution. The enzyme adopts the (beta/alpha)(8) fold common to the members of glycohydrolase family GH5. The structure is comparable with those of the homologous Trichoderma reesei and Thermomonospora fusca beta-mannanases: There is a conserved three-stranded beta-sheet located near the N terminus that stacks against the central beta-barrel at the end opposite the active site. Three noncanonical beta-helices surround the active site. Similar helices are found in T. reesei but not T. fusca beta-mannanase. By analogy with other beta-mannanases, the catalytic acid/base residue is E204 and the nucleophile residue is E318. The active site cleft of L. esculentum beta-mannanase most closely resembles that of the T. reesei isozyme. A model of substrate binding in LeMAN4a is proposed in which the mannosyl residue occupying the -1 subsite of the enzyme adopts the (1)S(5) skew-boat conformation.

SUBMITTER: Bourgault R 

PROVIDER: S-EPMC2253274 | biostudies-literature | 2005 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Three-dimensional structure of (1,4)-beta-D-mannan mannanohydrolase from tomato fruit.

Bourgault Richard R   Oakley Aaron J AJ   Bewley J Derek JD   Wilce Matthew C J MC  

Protein science : a publication of the Protein Society 20050501 5


The three-dimensional crystal structure of tomato (Lycopersicon esculentum) beta-mannanase 4a (LeMAN4a) has been determined to 1.5 A resolution. The enzyme adopts the (beta/alpha)(8) fold common to the members of glycohydrolase family GH5. The structure is comparable with those of the homologous Trichoderma reesei and Thermomonospora fusca beta-mannanases: There is a conserved three-stranded beta-sheet located near the N terminus that stacks against the central beta-barrel at the end opposite th  ...[more]

Similar Datasets

| S-EPMC4460921 | biostudies-literature
| S-EPMC1570163 | biostudies-literature
2013-04-05 | GSE42783 | GEO
2013-04-05 | E-GEOD-42783 | biostudies-arrayexpress
| S-EPMC2365515 | biostudies-literature
| S-EPMC5894362 | biostudies-literature
| S-EPMC3350922 | biostudies-literature
| S-EPMC4134323 | biostudies-literature
| S-EPMC2780388 | biostudies-literature
| S-EPMC2868798 | biostudies-literature