› 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 entry 5k5c coloured by chain, front view.
PDB entry 5k5c coloured by chain, side view.
PDB entry 5k5c coloured by chain, top view.
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:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102850 (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)

Quick links

Citations

3 citation in other articles

A fragment-based approach to assess the ligandability of ArgB, ArgC, ArgD and ArgF in the L-arginine biosynthetic pathway of Mycobacterium tuberculosis.
Gupta et al. (2021)
2 more

1 mention without citation

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