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Structure prediction and fold recognition for the ferrochelatase family of proteins
Author(s) -
Hansson M.,
Gough S.P.,
Brody S.S.
Publication year - 1997
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199704)27:4<517::aid-prot5>3.0.co;2-7
Subject(s) - ferrochelatase , protein secondary structure , computational biology , protein structure , protein superfamily , protein data bank , modeller , biology , chemistry , genetics , biochemistry , enzyme , homology modeling , gene , heme
An α/β 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. © 1997 Wiley‐Liss Inc.