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Open data
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Basic information
Entry | Database: PDB / ID: 6s6z | ||||||
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Title | Structure of beta-Galactosidase from Thermotoga maritima | ||||||
![]() | Beta-galactosidase | ||||||
![]() | HYDROLASE / BETA-GALACTOSIDASE / CARBOHYDRATE / GLUCOSYL HYDROLASE / THERMOTOGA MARITIMA / TRANSGLYCOSYLATION / IMMOBILIZATION / CRYOEM / GRAPHENE-OXIDE / GALACTOOLIGOSACCHARIDES | ||||||
Function / homology | ![]() lactose catabolic process / beta-galactosidase complex / beta-galactosidase / beta-galactosidase activity / carbohydrate binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2 Å | ||||||
![]() | Miguez-Amil, S. / Jimenez-Ortega, E. / Ramirez Escudero, M. / Sanz-Aparicio, J. / Fernandez-Leiro, R. | ||||||
![]() | ![]() Title: The cryo-EM Structure of β-Galactosidase: Quaternary Structure Guides Protein Engineering. Authors: Samuel Míguez Amil / Elena Jiménez-Ortega / Mercedes Ramírez-Escudero / David Talens-Perales / Julia Marín-Navarro / Julio Polaina / Julia Sanz-Aparicio / Rafael Fernandez-Leiro / ![]() Abstract: Lactose intolerance is a common digestive disorder that affects a large proportion of the adult human population. The severity of the symptoms is highly variable, depending on the susceptibility to ...Lactose intolerance is a common digestive disorder that affects a large proportion of the adult human population. The severity of the symptoms is highly variable, depending on the susceptibility to the sugar and the amount digested. For that reason, enzymes that can be used for the production of lactose-free milk and milk derivatives have acquired singular biotechnological importance. One such case is β-galactosidase (TmLac). Here, we report the cryo-EM structure of TmLac at 2.0 Å resolution. The protein features a newly solved domain at its C-terminus, characteristic of the genus , which promotes a peculiar octameric arrangement. We have assessed the constraints imposed by the quaternary protein structure on the construction of hybrid versions of this GH2 enzyme. Carbohydrate binding modules (CBM) from the CBM2 and CBM9 families have been added at either the amino or carboxy terminus, and the structural and functional effects of such modifications have been analyzed. The results provide a basis for the rational design of hybrid enzymes that can be efficiently attached to different solid supports. | ||||||
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 1.7 MB | Display | ![]() |
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PDB format | ![]() | 1.4 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 10109MC ![]() 6sd0C M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Assembly
Deposited unit | ![]()
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: _ / Beg auth comp-ID: PRO / Beg label comp-ID: PRO / End auth comp-ID: ARG / End label comp-ID: ARG / Refine code: _ / Auth seq-ID: 2 - 1084 / Label seq-ID: 1 - 1083
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