6bm9: Difference between revisions
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==Directed evolutionary changes in MBL super family - VIM-2 Round 10== | ==Directed evolutionary changes in MBL super family - VIM-2 Round 10== | ||
<StructureSection load='6bm9' size='340' side='right' caption='[[6bm9]], [[Resolution|resolution]] 2.19Å' scene=''> | <StructureSection load='6bm9' size='340' side='right'caption='[[6bm9]], [[Resolution|resolution]] 2.19Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6bm9]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BM9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BM9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6bm9]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BM9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BM9 FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 6bm9" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6bm9" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Carr, P D]] | [[Category: Carr, P D]] | ||
[[Category: Hong, N S]] | [[Category: Hong, N S]] | ||
Revision as of 11:35, 8 January 2020
Directed evolutionary changes in MBL super family - VIM-2 Round 10Directed evolutionary changes in MBL super family - VIM-2 Round 10
Structural highlights
Publication Abstract from PubMedGenetic variation among orthologous proteins can cause cryptic phenotypic properties that only manifest in changing environments. Such variation may impact the evolvability of proteins, but the underlying molecular basis remains unclear. Here, we performed comparative directed evolution of four orthologous metallo-beta-lactamases toward a new function and found that different starting genotypes evolved to distinct evolutionary outcomes. Despite a low initial fitness, one ortholog reached a significantly higher fitness plateau than its counterparts, via increasing catalytic activity. By contrast, the ortholog with the highest initial activity evolved to a less-optimal and phenotypically distinct outcome through changes in expression, oligomerization and activity. We show how cryptic molecular properties and conformational variation of active site residues in the initial genotypes cause epistasis, that could lead to distinct evolutionary outcomes. Our work highlights the importance of understanding the molecular details that connect genetic variation to protein function to improve the prediction of protein evolution. Cryptic genetic variation shapes the adaptive evolutionary potential of enzymes.,Baier F, Hong N, Yang G, Pabis A, Miton CM, Barrozo A, Carr PD, Kamerlin SC, Jackson CJ, Tokuriki N Elife. 2019 Feb 5;8. pii: 40789. doi: 10.7554/eLife.40789. PMID:30719972[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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