%0 Journal Article %1 Tripathi.200806 %A Tripathi, Timir %A Rahlfs, Stefan %A Becker, Katja %A Bhakuni, Vinod %D 2008/06// %J Biochim Biophys Acta %K Amino_Acid Amino_Acid_Sequence Animals Circular_Dichroism Glutaredoxins IFZ Molecular_Sequence_Data Molecular_Weight Plasmodium_falciparum Protein_Binding Protein_Denaturation Protons Protozoan_Proteins Sequence_Homology Temperature %N 6 %P 946-952 %T Structural and stability characteristics of a monothiol glutaredoxin: glutaredoxin-like protein 1 from Plasmodium falciparum %V 1784 %X Recently discovered monothiol glutaredoxins with CXXS-active site sequence share a common structural motif and biochemical mechanism of action and are involved in multiple cellular functions. Here we report first studies on the structural and stability characterization of a monothiol glutaredoxin, in particular--PfGLP1. Our results demonstrate that in the native conformation, the enzyme has a compact core structure with a relatively flexible N-terminal portion having an open configuration. Comparative functional studies with the full-length and N-terminal truncated protein demonstrate that the flexible N-terminal portion does not play any significant role in functional activity of the protein. In contrast to other Grxs, PfGLP1 does not contain a Fe-S cluster. The pH dependent studies demonstrate that the protein is resistant to alkaline pH but highly sensitive to acidic pH and undergoes significant unfolding between pH 4 and 5. However, acidic conditions also do not induce complete unf

@article{Tripathi.200806, abstract = {Recently discovered monothiol glutaredoxins with CXXS-active site sequence share a common structural motif and biochemical mechanism of action and are involved in multiple cellular functions. Here we report first studies on the structural and stability characterization of a monothiol glutaredoxin, in particular--PfGLP1. Our results demonstrate that in the native conformation, the enzyme has a compact core structure with a relatively flexible N-terminal portion having an open configuration. Comparative functional studies with the full-length and N-terminal truncated protein demonstrate that the flexible N-terminal portion does not play any significant role in functional activity of the protein. In contrast to other Grxs, PfGLP1 does not contain a Fe-S cluster. The pH dependent studies demonstrate that the protein is resistant to alkaline pH but highly sensitive to acidic pH and undergoes significant unfolding between pH 4 and 5. However, acidic conditions also do not induce complete unf}, added-at = {2008-10-14T16:07:18.000+0200}, author = {Tripathi, Timir and Rahlfs, Stefan and Becker, Katja and Bhakuni, Vinod}, biburl = {https://www.bibsonomy.org/bibtex/2f7da19c92c1723c8c603d5019cf616ec/nutribiochem}, interhash = {77215f346e3cf72265b3785720f76246}, intrahash = {f7da19c92c1723c8c603d5019cf616ec}, issn = {0006-3002}, journal = {Biochim Biophys Acta}, keywords = {Amino_Acid Amino_Acid_Sequence Animals Circular_Dichroism Glutaredoxins IFZ Molecular_Sequence_Data Molecular_Weight Plasmodium_falciparum Protein_Binding Protein_Denaturation Protons Protozoan_Proteins Sequence_Homology Temperature}, number = 6, pages = {946-952}, timestamp = {2008-10-14T16:08:42.000+0200}, title = {Structural and stability characteristics of a monothiol glutaredoxin: glutaredoxin-like protein 1 from Plasmodium falciparum}, volume = 1784, year = {2008/06//} }