Hinge-shift mechanism as a protein design principle for the evolution of β-lactamases from substrate promiscuity to specificity
TEM-1 β-lactamase evolved from ancestral enzymes that degraded a variety of β-lactam antibiotics with moderate efficiency and degrades β-lactam antibiotics with a strong preference for penicillins. Here authors developed a computational approach to rationally mold a protein flexibility profile on th...
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Nature Portfolio
2021
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oai:doaj.org-article:9f68b130500b474887f6a03663bb2f122021-12-02T11:44:56ZHinge-shift mechanism as a protein design principle for the evolution of β-lactamases from substrate promiscuity to specificity10.1038/s41467-021-22089-02041-1723https://doaj.org/article/9f68b130500b474887f6a03663bb2f122021-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-22089-0https://doaj.org/toc/2041-1723TEM-1 β-lactamase evolved from ancestral enzymes that degraded a variety of β-lactam antibiotics with moderate efficiency and degrades β-lactam antibiotics with a strong preference for penicillins. Here authors developed a computational approach to rationally mold a protein flexibility profile on the basis of a hinge-shift mechanism and show a putative Precambrian β-lactamase that mimics the modern TEM-1 β-lactamase with only 21 amino acid replacements.Tushar ModiValeria A. RissoSergio Martinez-RodriguezJose A. GaviraMubark D. MebratWade D. Van HornJose M. Sanchez-RuizS. Banu OzkanNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-14 (2021) |
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Science Q Tushar Modi Valeria A. Risso Sergio Martinez-Rodriguez Jose A. Gavira Mubark D. Mebrat Wade D. Van Horn Jose M. Sanchez-Ruiz S. Banu Ozkan Hinge-shift mechanism as a protein design principle for the evolution of β-lactamases from substrate promiscuity to specificity |
description |
TEM-1 β-lactamase evolved from ancestral enzymes that degraded a variety of β-lactam antibiotics with moderate efficiency and degrades β-lactam antibiotics with a strong preference for penicillins. Here authors developed a computational approach to rationally mold a protein flexibility profile on the basis of a hinge-shift mechanism and show a putative Precambrian β-lactamase that mimics the modern TEM-1 β-lactamase with only 21 amino acid replacements. |
format |
article |
author |
Tushar Modi Valeria A. Risso Sergio Martinez-Rodriguez Jose A. Gavira Mubark D. Mebrat Wade D. Van Horn Jose M. Sanchez-Ruiz S. Banu Ozkan |
author_facet |
Tushar Modi Valeria A. Risso Sergio Martinez-Rodriguez Jose A. Gavira Mubark D. Mebrat Wade D. Van Horn Jose M. Sanchez-Ruiz S. Banu Ozkan |
author_sort |
Tushar Modi |
title |
Hinge-shift mechanism as a protein design principle for the evolution of β-lactamases from substrate promiscuity to specificity |
title_short |
Hinge-shift mechanism as a protein design principle for the evolution of β-lactamases from substrate promiscuity to specificity |
title_full |
Hinge-shift mechanism as a protein design principle for the evolution of β-lactamases from substrate promiscuity to specificity |
title_fullStr |
Hinge-shift mechanism as a protein design principle for the evolution of β-lactamases from substrate promiscuity to specificity |
title_full_unstemmed |
Hinge-shift mechanism as a protein design principle for the evolution of β-lactamases from substrate promiscuity to specificity |
title_sort |
hinge-shift mechanism as a protein design principle for the evolution of β-lactamases from substrate promiscuity to specificity |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/9f68b130500b474887f6a03663bb2f12 |
work_keys_str_mv |
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