› 4ksa

X-ray diffraction
2.7Å resolution

Crystal Structure of Malonyl-CoA decarboxylase from Rhodopseudomonas palustris, Northeast Structural Genomics Consortium Target RpR127

Released:
DOI: 10.2210/pdb4ksa/pdb
PDB entry 4ksa coloured by chain, front view.
PDB entry 4ksa coloured by chain, side view.
PDB entry 4ksa coloured by chain, top view.
Source organism: Rhodopseudomonas palustris CGA009
Primary publication:
Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations.
Froese DS, Forouhar F, Tran TH, Vollmar M, Kim YS, Lew S, Neely H, Seetharaman J, Shen Y, Xiao R, Acton TB, Everett JK, Cannone G, Puranik S, Savitsky P, Krojer T, Pilka ES, Kiyani W, Lee WH, Marsden BD, von Delft F, Allerston CK, Spagnolo L, Gileadi O, Montelione GT, Oppermann U, Yue WW, Tong L
Structure 21 1182-92 (2013)
PMID: 23791943

Function and Biology Details

Reaction catalysed: 
Malonyl-CoA = acetyl-CoA + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180006 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Malonyl-CoA decarboxylase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 453 amino acids
Theoretical weight: 50.39 KDa
Source organism: Rhodopseudomonas palustris CGA009
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6NCB2 (Residues: 8-451; Coverage: 93%)
Gene names: MLYCD/MCD, RPA0560
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand MG 2 x MG
1 modified residue:
Ligand MSE 20 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: P21212
Unit cell:
a: 141.505Å b: 159.765Å c: 108.622Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.225 0.279
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

From structural biology to designing therapy for inborn errors of metabolism.
Yue WW. (2016)
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