scholarly journals Evolutionary dynamics of modular polyketide synthases, with implications for protein design and engineering

2010 ◽  
Vol 64 (1) ◽  
pp. 89-92 ◽  
Author(s):  
Jurica Zucko ◽  
John Cullum ◽  
Daslav Hranueli ◽  
Paul F Long
2019 ◽  
Vol 28 (3) ◽  
pp. 672-672
Author(s):  
Connie Y. Wang ◽  
Paul M. Chang ◽  
Marie L. Ary ◽  
Benjamin D. Allen ◽  
Roberto A. Chica ◽  
...  

2002 ◽  
Vol 31 (6) ◽  
pp. 335-341 ◽  
Author(s):  
Nicholas C. Yoder ◽  
Krishna Kumar

Science ◽  
2020 ◽  
Vol 371 (6524) ◽  
pp. 86-90
Author(s):  
Acacia F. Dishman ◽  
Robert C. Tyler ◽  
Jamie C. Fox ◽  
Andrew B. Kleist ◽  
Kenneth E. Prehoda ◽  
...  

Metamorphic proteins switch between different folds, defying the protein folding paradigm. It is unclear how fold switching arises during evolution. With ancestral reconstruction and nuclear magnetic resonance, we studied the evolution of the metamorphic human protein XCL1, which has two distinct folds with different functions, making it an unusual member of the chemokine family, whose members generally adopt one conserved fold. XCL1 evolved from an ancestor with the chemokine fold. Evolution of a dimer interface, changes in structural constraints and molecular strain, and alteration of intramolecular protein contacts drove the evolution of metamorphosis. Then, XCL1 likely evolved to preferentially populate the noncanonical fold before reaching its modern-day near-equal population of folds. These discoveries illuminate how one sequence has evolved to encode multiple structures, revealing principles for protein design and engineering.


Author(s):  
Christian Renner ◽  
Stefan Alefelder ◽  
Jae H. Bae ◽  
Nediljko Budisa ◽  
Robert Huber ◽  
...  

2018 ◽  
Vol 27 (6) ◽  
pp. 1113-1124 ◽  
Author(s):  
Connie Y. Wang ◽  
Paul M. Chang ◽  
Marie L. Ary ◽  
Benjamin D. Allen ◽  
Roberto A. Chica ◽  
...  

2016 ◽  
Vol 110 (3) ◽  
pp. 345a
Author(s):  
Christine Koehler ◽  
Paul Sauter ◽  
Mirella Wawryszyn ◽  
Gemma Estrada Girona ◽  
Markus H. Fritz ◽  
...  

2017 ◽  
Vol 61 (2) ◽  
pp. 245-258 ◽  
Author(s):  
Lewis A. Churchfield ◽  
Athira George ◽  
F. Akif Tezcan

Inspired by the remarkable sophistication and complexity of natural metalloproteins, the field of protein design and engineering has traditionally sought to understand and recapitulate the design principles that underlie the interplay between metals and protein scaffolds. Yet, some recent efforts in the field demonstrate that it is possible to create new metalloproteins with structural, functional and physico-chemical properties that transcend evolutionary boundaries. This essay aims to highlight some of these efforts and draw attention to the ever-expanding scope of bioinorganic chemistry and its new connections to synthetic biology, biotechnology, supramolecular chemistry and materials engineering.


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