A theoretical model of Aquifex pyrophilus flagellin: implications for its thermostability.
Aquifex pyrophilus is a flagellated hyperthermophilic eubacterial species that grows optimally at 85 degrees C. The thermostable A. pyrophilus flagellar filament is primarily composed of a single protein called flagellin (FlaA). The N- and C-terminal sequence regions of FlaA are important for self-assembly and share high sequence similarity with mesophilic bacterial flagellins. We have developed a predictive 3D-structure of FlaA, using the published structure of mesophilic Salmonella typhimurium flagellin (FliC) as a template and analyzed it with respect to possible determinants of thermostability. A sequence comparison of FlaA and FliC revealed a +7.0% increase in FlaA hydrophobic residues, a +0.6% increase in charged residues and a corresponding decrease of -6.0% in polar residues. The FlaA N- and C-termini also have higher proportions of hydrophobic and charged residues at the expense of polar residues and higher non-polar surface areas. Thus, a predominant stabilizing factor in FlaA appears to be increased hydrophobicity, which often confers greater rigidity to proteins. Fewer intramolecular ion pairs were observed in FlaA than FliC, although an increase in the positive charge potential of the FlaA D0 and D1 domains was also observed; increased intermolecular salt bridges may also contribute to the thermal stability of the oligomeric flagellar fiber. [Figure: see text].
Malapaka
V Raghu Ram
VR
Department of Biological Sciences, Mailstop 5410, 1903 West Michigan Avenue, Western Michigan University, Kalamazoo, MI 49008-5410, USA.
Tripp
Brian C
BC
D000595:Amino Acid Sequence; D017124:Conserved Sequence; D005408:Flagellin / Q000737:chemistry / Q000378:metabolism*; D057927:Hydrophobic and Hydrophilic Interactions; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011489:Protein Denaturation; D020836:Protein Structure, Quaternary; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D040681:Structural Homology, Protein; D013696:Temperature
D021122:Protein Subunits; D005408:Flagellin