8X3U | pdb_00008x3u

tll1591 with alpha_glucan 3sugar


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.58 Å
  • R-Value Free: 
    0.304 (Depositor), 0.300 (DCC) 
  • R-Value Work: 
    0.277 (Depositor), 0.276 (DCC) 
  • R-Value Observed: 
    0.278 (Depositor) 

Starting Model: experimental
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This is version 1.1 of the entry. See complete history


Literature

Glucosyltransferase TeGSS from Thermosynechococcus elongatus produces an alpha-1,2-glucan.

Qu, X.An, Q.Sayed, H.Cui, L.Mayo, K.H.Su, J.Y.

(2024) Int J Biol Macromol 280: 136152-136152

  • DOI: https://doi.org/10.1016/j.ijbiomac.2024.136152
  • Primary Citation of Related Structures:  
    8X3Q, 8X3U

  • PubMed Abstract: 

    Here, we enzymatically produced a novel α-1,2-glucan, glucosylsucrose, that has a chemical structure significantly different from that of other glucans. This structural difference suggests its potential to modulate new physiological activities compared to known glucans. The enzyme TeGSS catalyzes the synthesis of this α-1,2-glucan from sucrose and UDP-glucose (UDPG). Using NMR spectroscopy, we elucidated the chemical structures of TeGSS-synthesized glucosylsucrose tri-, tetra-, and penta-saccharides in which the monosaccharide units are linked by α-1,2-glycosidic bonds. We also report the crystal structures of TeGSS co-crystallized with UDP and glucosylsucrose tri- and tetra-saccharides. Site-directed mutagenesis of residues in and around the TeGSS catalytic center has allowed us to propose a concerted S N i mechanism of action. Finally, we developed an enzyme-coupled reaction involving TeGSS and SuSyAc that allows production of UDPG for the synthesis of α-1,2-glucan.


  • Organizational Affiliation

    Engineering Research Center of Glycoconjugates Ministry of Education, Jilin Provincial Key Laboratory of Chemistry and Biology of Changbai Mountain Natural Drugs, School of Life Sciences, Northeast Normal University, Changchun 130024, China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Glycosyl transferaseA [auth B],
B [auth A],
C,
D
361Thermosynechococcus vestitus BP-1Mutation(s): 0 
Gene Names: tll1591
UniProt
Find proteins for Q8DIJ4 (Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1))
Explore Q8DIJ4 
Go to UniProtKB:  Q8DIJ4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8DIJ4
Sequence Annotations
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  • Reference Sequence
Oligosaccharides

Help

Entity ID: 2
MoleculeChains Length2D Diagram Glycosylation3D Interactions
alpha-D-glucopyranose-(1-2)-alpha-D-glucopyranose-(1-2)-beta-D-fructofuranose
E, F, G, H
3N/A
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.58 Å
  • R-Value Free:  0.304 (Depositor), 0.300 (DCC) 
  • R-Value Work:  0.277 (Depositor), 0.276 (DCC) 
  • R-Value Observed: 0.278 (Depositor) 
Space Group: P 65
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 156.135α = 90
b = 156.135β = 90
c = 187.561γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement

Structure Validation

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Entry History & Funding Information

Deposition Data

  • Released Date: 2024-10-16 
  • Deposition Author(s): Su, J.Y.

Funding OrganizationLocationGrant Number
National Natural Science Foundation of China (NSFC)China32171255

Revision History  (Full details and data files)

  • Version 1.0: 2024-10-16
    Type: Initial release
  • Version 1.1: 2025-04-30
    Changes: Database references