› 3s28

X-ray diffraction
2.8Å resolution

The crystal structure of sucrose synthase-1 in complex with a breakdown product of the UDP-glucose

Released:
DOI: 10.2210/pdb3s28/pdb
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PDB entry 3s28 coloured by chain, front view.
PDB entry 3s28 coloured by chain, side view.
PDB entry 3s28 coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
The structure of sucrose synthase-1 from Arabidopsis thaliana and its functional implications.
Zheng Y, Anderson S, Zhang Y, Garavito RM
J Biol Chem 286 36108-36118 (2011)
PMID: 21865170

Function and Biology Details

Reaction catalysed: 
NDP-glucose + D-fructose = NDP + sucrose
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155847 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sucrose synthase 1 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 816 amino acids
Theoretical weight: 94.18 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P49040 (Residues: 1-808; Coverage: 100%)
Gene names: At5g20830, SUS1, T1M15.230
Sequence domains:
Structure domains:

Ligands and Environments

6 bound ligands:
Ligand UDP 8 x UDP
Ligand LCN 8 x LCN
Ligand NHF 8 x NHF
Ligand SO4 24 x SO4
Ligand MLA 8 x MLA
Ligand K 8 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: C2
Unit cell:
a: 276.75Å b: 261.88Å c: 160.19Å
α: 90° β: 108.7° γ: 90°
R-values:
R R work R free
0.19 0.188 0.236
Expression system: Escherichia coli BL21(DE3)

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Citations

7 review citations

An Overview of Sucrose Synthases in Plants.
Stein et al. (2019)
6 more

5 mentions without citation

Identification of UDP-glucose binding site in glycosyltransferase domain of sucrose phosphate synthase from sugarcane (Saccharum officinarum) by structure-based site-directed mutagenesis.
Sawitri et al. (2018)
4 more

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