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| [[Image:2eu8.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2eu8| PDB=2eu8 | SCENE= }} | | {{STRUCTURE_2eu8| PDB=2eu8 | SCENE= }} |
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| '''Crystal structure of a thermostable mutant of Bacillus subtilis Adenylate Kinase (Q199R)'''
| | ===Crystal structure of a thermostable mutant of Bacillus subtilis Adenylate Kinase (Q199R)=== |
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| ==Overview==
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| In nature, evolution occurs through the continuous adaptation of a population to its environment. At the molecular level, adaptive changes in protein sequence and expression impact organismal fitness and, consequently, dictate population dynamics. Here, we have used a "weak link" method to favor variations in one gene, allowing adaptation to thermostability to be studied in molecular detail as bacteria were grown continuously for approximately 1500 generations. Surprisingly, only six mutant alleles, representing less than 1% of the possible missense mutations, were observed, suggesting a highly constrained molecular landscape during protein evolution. The changes in organismal fitness were linked directly to incremental increases in enzyme stability and activity maxima and corresponded to the narrow temperature ranges where each mutant enjoyed success within the overall population. Thus, continuous evolution of a single gene permits a quantitative approach that extends from the phenotypes of the microbial populations to their underlying biophysical basis.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16713575}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16713575 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16713575}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Point mutant]] | | [[Category: Point mutant]] |
| [[Category: Thermostability]] | | [[Category: Thermostability]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:07:08 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:00:11 2008'' |
