› 5k5c

X-ray diffraction
1.85Å resolution

Structure of Mycobacterium thermoresistibile trehalose-6-phosphate synthase in a complex with Trehalose.

Released:
DOI: 10.2210/pdb5k5c/pdb
PDB 5k5c coloured by chain and viewed from the front.
PDB 5k5c coloured by chain and viewed from the side.
PDB 5k5c coloured by chain and viewed from the top.
Source organism: Mycolicibacterium thermoresistibile
Primary publication:
Mycobacterial OtsA Structures Unveil Substrate Preference Mechanism and Allosteric Regulation by 2-Oxoglutarate and 2-Phosphoglycerate.
Mendes V, Acebrón-García-de-Eulate M, Verma N, Blaszczyk M, Dias MVB, Blundell TL
mBio 10 (2019)
PMID: 31772052

Function and Biology Details

Reaction catalysed: 
ADP-alpha-D-glucose + D-glucose 6-phosphate = ADP + alpha,alpha-trehalose 6-phosphate
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Alpha,alpha-trehalose-phosphate synthase (ADP-forming) Chain: A
Molecule details ›
Chain: A
Length: 487 amino acids
Theoretical weight: 54.68 KDa
Source organism: Mycolicibacterium thermoresistibile
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A117IMA6 (Residues: 1-486; Coverage: 100%)
Gene name: RMCT_1906
Sequence domains: Glycosyltransferase family 20
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
2 bound ligands:
Ligand NHE 2 x NHE
Ligand EDO 8 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: I4122
Unit cell:
a: 127.318Å b: 127.318Å c: 207.387Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.152 0.151 0.175
Expression system: Escherichia coli BL21(DE3)

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Citations

1 mention without citation

Mycobacterial OtsA Structures Unveil Substrate Preference Mechanism and Allosteric Regulation by 2-Oxoglutarate and 2-Phosphoglycerate.
Mendes et al. (2019)