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Haloadaptation: insights from comparative modeling studies of halophilic archaeal DHFRs.

Abstract：

:Proteins of halophilic archaea function in high-salt concentrations that inactivate or precipitate homologous proteins from non-halophilic species. Haloadaptation and the mechanism behind the phenomenon are not yet fully understood. In order to obtain useful information, homology modeling studies of dihydrofolate reductases (DHFRs) from halophilic archaea were performed that led to the construction of structural models. These models were subjected to energy minimization, structural evaluation and analysis. Complementary approaches concerning calculations of the amino acid composition and visual inspection of the surfaces and cores of the models, as well as calculations of electrostatic surface potentials, in comparison to non-halophilic DHFRs were also performed. The results provide evidence that sheds some light on the phenomenon of haloadaptation: DHFRs from halophilic archaea may maintain their fold, in high-salt concentrations, by sharing highly negatively charged surfaces and weak hydrophobic cores.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Kastritis PL,Papandreou NC,Hamodrakas SJ

doi

10.1016/j.ijbiomac.2007.06.005

subject

Has Abstract

pub_date

2007-10-01 00:00:00

pages

447-53

issue

4

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(07)00147-X

journal_volume

41

pub_type

杂志文章

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