Structure prediction and fold recognition for the ferrochelatase family of proteins
(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:
https://lup.lub.lu.se/record/8001527
- author
- Hansson, Mats LU ; Gough, S. P. and Brody, S. S.
- publishing date
- 1997
- 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 Inc.
- 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
- additional info
- 4
- id
- 39c0352a-86e6-4fd2-94d3-6ee74473dd54 (old id 8001527)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/9141132
- date added to LUP
- 2016-04-01 16:18:47
- date last changed
- 2022-01-28 18:50:23
@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}}, 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}}, language = {{eng}}, number = {{4}}, pages = {{517--522}}, publisher = {{John Wiley & Sons Inc.}}, 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}}, doi = {{10.1002/(SICI)1097-0134(199704)27:4<517::AID-PROT5>3.0.CO;2-7}}, volume = {{27}}, year = {{1997}}, }