6S6Z

Structure of beta-Galactosidase from Thermotoga maritima


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.00 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

The cryo-EM Structure ofThermotoga maritimabeta-Galactosidase: Quaternary Structure Guides Protein Engineering.

Miguez Amil, S.Jimenez-Ortega, E.Ramirez-Escudero, M.Talens-Perales, D.Marin-Navarro, J.Polaina, J.Sanz-Aparicio, J.Fernandez-Leiro, R.

(2020) ACS Chem Biol 15: 179-188

  • DOI: https://doi.org/10.1021/acschembio.9b00752
  • Primary Citation of Related Structures:  
    6S6Z, 6SD0

  • PubMed 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 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 Thermotoga maritima 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 Thermotoga , 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.


  • Organizational Affiliation

    Spanish National Cancer Research Centre (CNIO) , Melchor Fernández Almagro 3 , 28029 , Madrid , Spain.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-galactosidase1,083Thermotoga maritima MSB8Mutation(s): 0 
Gene Names: lacZTM_1193
EC: 3.2.1.23
UniProt
Find proteins for Q56307 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8))
Explore Q56307 
Go to UniProtKB:  Q56307
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ56307
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.00 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONRELION3.0
MODEL REFINEMENTCoot0.9-pre
MODEL REFINEMENTREFMAC5.5.0026

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2020-03-18
    Type: Initial release
  • Version 1.1: 2024-05-22
    Changes: Data collection, Database references, Refinement description