Molecular cloning, expression, purification and characterization of a recombinant FKBP family member from Pseudomonas aeruginosa.
The FK-506 binding proteins (FKBPs) are a family of proteins with characterised molecular functions such as peptidylprolyl cis-trans isomerase activity and chaperone activity. However, the FKBP family member from Pseudomonas aeruginosa is currently uncharacterised. This study has successfully develo...
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| Format: | Final Year Project |
| Language: | English |
| Published: |
2010
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| Online Access: | http://hdl.handle.net/10356/39981 |
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| Institution: | Nanyang Technological University |
| Language: | English |
| Summary: | The FK-506 binding proteins (FKBPs) are a family of proteins with characterised molecular functions such as peptidylprolyl cis-trans isomerase activity and chaperone activity. However, the FKBP family member from Pseudomonas aeruginosa is currently uncharacterised. This study has successfully developed a recombinant method of overexpressing and purifying the FK-506 binding domain of P. aeruginosa (PaFKBD) in a SUMO-PaFKBD fusion protein state. The characterisation of SUMO-PaFKBD revealed peptidylprolyl cis-trans isomerase activity with catalytic efficiency of 1.01 x 105 s-1 M-1 and this activity is inhibited by FK-506 with an IC50 of 92.6nM. More studies need to be done to further reaffirm these results and to further characterise the protein. |
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