Structure prediction and fold recognition for the ferrochelatase family of proteins.
An alpha/beta barrel is predicted for the three-dimensional (3D) structure of Bacillus subtilis ferrochelatase. To arrive at this structure, the THREADER program was used to find possible homologous 3D structures and to predict the secondary structure for the ferrochelatase sequence. The secondary structure was fit by hand to the selected homologous 3D structure then the MODELLER program was used to predict the fold of ferrochelatase. Molecular biological information about the conserved residues of ferrochelatase was used as the criteria to help select the homologous 3D structure used to predict the fold of ferrochelatase. Based on the predicted structure possible, ligands binding to the iron and protoporphyrin IX are discussed. The structure has been deposited in the Brookhaven database as ID 1FJI.
Hansson
M
M
Carlsberg Laboratory, Department of Physiology, Copenhagen Valby, Denmark.
Gough
S P
SP
Brody
S S
SS
D000465:Algorithms; D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology; D003198:Computer Simulation; D005294:Ferrochelatase / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment / Q000379:methods; D017386:Sequence Homology, Amino Acid
D005294:Ferrochelatase