› 3t57

X-ray diffraction
2.1Å resolution

Activity and Crystal Structure of Arabidopsis UDP-N-acetylglucosamine acyltransferase

Released:
DOI: 10.2210/pdb3t57/pdb
PDB entry 3t57 coloured by chain, front view.
PDB entry 3t57 coloured by chain, side view.
PDB entry 3t57 coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Activity and crystal structure of Arabidopsis thaliana UDP-N-acetylglucosamine acyltransferase.
Joo SH, Chung HS, Raetz CR, Garrett TA
Biochemistry 51 4322-30 (2012)
PMID: 22545860

Function and Biology Details

Reaction catalysed: 
A (3R)-3-hydroxyacyl-[acyl-carrier-protein] + UDP-N-acetyl-alpha-D-glucosamine = an [acyl-carrier-protein] + a UDP-3-O-(3-hydroxyacylyl)-N-acetyl-alpha-D-glucosamine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193541 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 305 amino acids
Theoretical weight: 33.28 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9SU91 (Residues: 33-336; Coverage: 91%)
Gene names: At4g29540, LPXA, T16L4.50
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P6322
Unit cell:
a: 86.195Å b: 86.195Å c: 200.25Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.207 0.241
Expression system: Escherichia coli

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Citations

1 review citation

Acyltransferases in bacteria.
Röttig et al. (2013)
4 other articles

1 mention without citation

Activity and crystal structure of Arabidopsis thaliana UDP-N-acetylglucosamine acyltransferase.
Joo et al. (2012)