› 2alm

X-ray diffraction
2.6Å resolution

Crystal structure analysis of a mutant beta-ketoacyl-[acyl carrier protein] synthase II from Streptococcus pneumoniae

Released:
DOI: 10.2210/pdb2alm/pdb
PDB entry 2alm coloured by chain, front view.
PDB entry 2alm coloured by chain, side view.
PDB entry 2alm coloured by chain, top view.
Source organism: Streptococcus pneumoniae
Primary publication:
Roles of the active site water, histidine 303, and phenylalanine 396 in the catalytic mechanism of the elongation condensing enzyme of Streptococcus pneumoniae.
Zhang YM, Hurlbert J, White SW, Rock CO
J Biol Chem 281 17390-17399 (2006)
PMID: 16618705

Function and Biology Details

Reaction catalysed: 
A (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a (Z)-3-oxooctadec-11-enoyl-[acyl-carrier protein] + CO(2) + an [acyl-carrier protein]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190278 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-oxoacyl-[acyl-carrier-protein] synthase 2 Chain: A
Molecule details ›
Chain: A
Length: 431 amino acids
Theoretical weight: 46.1 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9FBC2 (Residues: 1-409; Coverage: 100%)
Gene names: A5N45_03205, AZJ28_03470, AZJ70_07650, AZK02_07750, ERS019209_01512, ERS019261_01074, ERS019316_01650, ERS019486_01303, ERS019694_00480, ERS020302_00911, ERS020893_01786, ERS020941_00999, ERS021218_01784, ERS043904_02518, ERS096071_01417, GM536_04995, GM539_04300, GM540_01020, GM543_03230, GM544_00755, GM545_01935, RLD18_05995, SAMEA1462998_00705, SAMEA2627268_00398, SAMEA3171064_01875, SAMEA3353485_01245, SAMEA3354366_00476, SAMEA3381574_00886, SAMEA3389245_02216, SAMEA3390019_00019, fabF, fabF_3
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments

1 bound ligand:
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21212
Unit cell:
a: 60.393Å b: 88.82Å c: 61.048Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.195 0.257
Expression system: Escherichia coli

Quick links

Citations

4 review citations

The type I fatty acid and polyketide synthases: a tale of two megasynthases.
Smith et al. (2007)
3 more

3 mentions without citation

Structural classification and properties of ketoacyl synthases.
Chen et al. (2011)
2 more