The X-ray crystal structure of beta-ketoacyl [acyl carrier protein] synthase I.
The crystal structure of the fatty acid elongating enzyme beta-ketoacyl [acyl carrier protein] synthase I (KAS I) from Escherichia coli has been determined to 2.3 A resolution by molecular replacement using the recently solved crystal structure of KAS II as a search model. The crystal contains two independent dimers in the asymmetric unit. KAS I assumes the thiolase alpha(beta)alpha(beta)alpha fold. Electrostatic potential distribution reveals an acyl carrier protein docking site and a presumed substrate binding pocket was detected extending the active site. Both subunits contribute to each substrate binding site in the dimer.
Olsen
J G
JG
Centre for Crystallographic Studies, University of Copenhagen, Denmark.
Kadziola
A
A
von Wettstein-Knowles
P
P
Siggaard-Andersen
M
M
Lindquist
Y
Y
Larsen
S
S
D000595:Amino Acid Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D019281:Dimerization; D004926:Escherichia coli; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry; D016415:Sequence Alignment; D055672:Static Electricity; D017855:Transferases (Other Substituted Phosphate Groups) / Q000737:chemistry*
D011994:Recombinant Proteins; D017855:Transferases (Other Substituted Phosphate Groups); C021364:holo-(acyl-carrier-protein) synthase