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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Thorbjarnardóttir, Sigríður H. Kristjánsson, Magnús M. Sigtryggsdóttir, Asta Rós Papaleo, Elena |
| Description | Author Affiliation: Sigtryggsdóttir AR ( Deparment of Biochemistry, Science Institute, University of Iceland, Reykjavík, Iceland.); Papaleo E ( Structural Biology and NMR Laboratory, Department of Biology, University of Copenhagen, Ole Maaloes Vej 5, DK-2200 Copenhagen, Denmark.); Thorbjarnardóttir SH ( Institute of Biology, University of Iceland, Reykjavík, Iceland.); Kristjánsson MM ( Deparment of Biochemistry, Science Institute, University of Iceland, Reykjavík, Iceland. Electronic address: mmk@hi.is.) |
| Abstract | The subtilisin-like serine proteinases, VPR, from a psychrotrophic Vibrio species and aqualysin I (AQUI) from the thermophile Thermus aquaticus , are structural homologues, but differ significantly with respect to stability and catalytic properties. It has been postulated that the higher catalytic activity of cold adapted enzymes when compared to homologues from thermophiles, reflects their higher molecular flexibility. To assess a potential difference in molecular flexibility between the two homologous proteinases, we have measured their Trp fluorescence quenching by acrylamide at different temperatures. We also investigated protein dynamics of VPR and AQUI at an atomic level by molecular dynamics simulations. VPR contains four Trp residues, three of which are at corresponding sites in the structure of AQUI. To aid in the comparison, a Tyr at the fourth corresponding site in AQUI was mutated to Trp (Y191W). A lower quenching effect of acrylamide on the intrinsic fluorescence of the thermophilic AQUI_Y191W was observed at all temperatures measured (10–55 °C), suggesting that it possesses a more rigid structure than VPR. The MD analysis (Cα rmsf profiles) showed that even though VPR and AQUI have similar flexibility profiles, the cold adapted VPR displays higher flexibility in most regions of the protein structure. Some of these regions contain or are in proximity to some of the Trp residues (Trp6, Trp114 and Trp208) in the proteins. Thus, we observe an overall agreement between the fluorescence quenching data and the flexibility profiles obtained from the MD simulations to different flexibilities of specific regions in the proteins. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 4 |
| Volume Number | 1844 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2014-04-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Bacterial Proteins Chemistry Molecular Dynamics Simulation Serine Endopeptidases Subtilisins Thermus Vibrio Amino Acid Substitution Genetics Cold Temperature Escherichia Coli Enzymology Fluorescence Gene Expression Hot Temperature Kinetics Pliability Protein Structure, Secondary Protein Structure, Tertiary Recombinant Proteins Tryptophan Tyrosine Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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