› 2xr7

X-ray diffraction
3.1Å resolution

Crystal Structure of Nicotiana tabacum malonyltransferase (NtMat1) complexed with malonyl-coa

Released:
DOI: 10.2210/pdb2xr7/pdb
PDB entry 2xr7 coloured by chain, front view.
PDB entry 2xr7 coloured by chain, side view.
PDB entry 2xr7 coloured by chain, top view.
Source organism: Nicotiana tabacum
Primary publication:
Structural basis for modification of flavonol and naphthol glucoconjugates by Nicotiana tabacum malonyltransferase (NtMaT1).
Manjasetty BA, Yu XH, Panjikar S, Taguchi G, Chance MR, Liu CJ
Planta 236 781-93 (2012)
PMID: 22610270

Function and Biology Details

Reaction catalysed: 
Malonyl-CoA + flavonol 3-O-beta-D-glucoside = CoA + flavonol 3-O-(6-O-malonyl-beta-D-glucoside)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176733 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenolic glucoside malonyltransferase 1 Chain: A
Molecule details ›
Chain: A
Length: 453 amino acids
Theoretical weight: 51.43 KDa
Source organism: Nicotiana tabacum
UniProt:
  • Canonical: Q589Y0 (Residues: 1-453; Coverage: 100%)
Gene name: mat1
Sequence domains: Transferase family
Structure domains: Chloramphenicol acetyltransferase-like domain

Ligands and Environments


Cofactor: Ligand MLC 1 x MLC
No bound ligands
1 modified residue:
Ligand MSE 13 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A, NSLS BEAMLINE X3A
Spacegroup: P42212
Unit cell:
a: 98.079Å b: 98.079Å c: 151.84Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.226 0.289

Quick links

Citations

1 review citation

Family characteristics, phylogenetic reconstruction, and potential applications of the plant BAHD acyltransferase family.
Xu et al. (2023)
7 other articles

1 mention without citation

Illuminating the biosynthesis pathway genes involved in bioactive specific monoterpene glycosides in Paeonia veitchii Lynch by a combination of sequencing platforms.
Zhang et al. (2023)