Structural highlights
Publication Abstract from PubMed
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.
Structure prediction and fold recognition for the ferrochelatase family of proteins.,Hansson M, Gough SP, Brody SS Proteins. 1997 Apr;27(4):517-22. PMID:9141132[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hansson M, Gough SP, Brody SS. Structure prediction and fold recognition for the ferrochelatase family of proteins. Proteins. 1997 Apr;27(4):517-22. PMID:9141132
