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Structure prediction and fold recognition for the ferrochelatase family of proteins

Hansson, Mats LU ; Gough, S. P. and Brody, S. S. (1997) In Proteins 27(4). p.517-522
Abstract
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Secondary, Sequence Homology, Sequence Alignment/methods, Tertiary, *Protein Structure, *Protein Folding, Molecular Sequence Data, Molecular, Models, Ferrochelatase/*chemistry, Computer Simulation, Bacillus subtilis/enzymology, Algorithms, Amino Acid Sequence, Amino Acid
in
Proteins
volume
27
issue
4
pages
517 - 522
publisher
John Wiley & Sons
external identifiers
  • scopus:0030920605
ISSN
0887-3585
DOI
10.1002/(SICI)1097-0134(199704)27:4<517::AID-PROT5>3.0.CO;2-7
language
English
LU publication?
no
id
39c0352a-86e6-4fd2-94d3-6ee74473dd54 (old id 8001527)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/9141132
date added to LUP
2015-10-01 09:32:41
date last changed
2017-01-01 07:01:46
@article{39c0352a-86e6-4fd2-94d3-6ee74473dd54,
  abstract     = {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.},
  author       = {Hansson, Mats and Gough, S. P. and Brody, S. S.},
  issn         = {0887-3585},
  keyword      = {Secondary,Sequence Homology,Sequence Alignment/methods,Tertiary,*Protein Structure,*Protein Folding,Molecular Sequence Data,Molecular,Models,Ferrochelatase/*chemistry,Computer Simulation,Bacillus subtilis/enzymology,Algorithms,Amino Acid Sequence,Amino Acid},
  language     = {eng},
  number       = {4},
  pages        = {517--522},
  publisher    = {John Wiley & Sons},
  series       = {Proteins},
  title        = {Structure prediction and fold recognition for the ferrochelatase family of proteins},
  url          = {http://dx.doi.org/10.1002/(SICI)1097-0134(199704)27:4<517::AID-PROT5>3.0.CO;2-7},
  volume       = {27},
  year         = {1997},
}