Homology modelling of the Frankia nitrogenase iron protein

The NifH protein contains an iron-sulfur cluster performing different functions during nitrogen fixation. Frankia is an actinomycete, entering into symbiotic association with a number of dicotyledonous plants and fixing nitrogen. The structure of the Frankia NifH protein was determined using homolog...

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Bibliographic Details
Published in:Symbiosis (Philadelphia, Pa.) Pa.), 2010-02, Vol.50 (1-2), p.37-44
Main Authors: Sen, Arnab, Sur, Saubashya, Tisa, Louis S, Bothra, Asim Kr, Thakur, Subarna, Mondal, Uttam Kr
Format: Article
Language:English
Subjects:
amino acid sequences
bacterial proteins
binding sites
Biomedical and Life Sciences
Developmental Biology
Ecology
Evolutionary Biology
Frankia
iron
iron protein
Life Sciences
Microbiology
NifH protein
nitrogen fixation
nitrogenase
Plant Sciences
protein structure
site-directed mutagenesis
sulfur
thiols
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Summary:The NifH protein contains an iron-sulfur cluster performing different functions during nitrogen fixation. Frankia is an actinomycete, entering into symbiotic association with a number of dicotyledonous plants and fixing nitrogen. The structure of the Frankia NifH protein was determined using homology modelling technique. Metal binding sites and functionally important regions of the protein were analyzed. Thiol ligands and active sites help in protein functioning and conformations. Structurally important nests were recognized. Clefts and cavities contain biologically important residues. Site-directed mutagenesis results reveal that mutations in functional residues hamper nitrogen fixation. The structure is rigid with an accessible surface for solvents. The structure is reliable offering insights into the 3D structural framework as well as structure-function relation of NifH protein.
ISSN:0334-5114
1878-7665
DOI:10.1007/s13199-009-0035-9