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==STRUCTURE OF FERROCHELATASE, THEORETICAL MODEL== | |||
<StructureSection load='1fji' size='340' side='right' caption='[[1fji]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FJI FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fji FirstGlance], [http://www.ebi.ac.uk/pdbsum/1fji PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:9141132</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Brody, S S]] | [[Category: Brody, S S]] | ||
[[Category: Gough, S P]] | [[Category: Gough, S P]] | ||
[[Category: Hansson, M]] | [[Category: Hansson, M]] |
Revision as of 15:47, 28 September 2014
STRUCTURE OF FERROCHELATASE, THEORETICAL MODELSTRUCTURE OF FERROCHELATASE, THEORETICAL MODEL
Structural highlights
Publication Abstract from PubMedAn 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 |
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