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@article{48195,
author = {Marková, Klára and Chmelová, Klaudia and Marques, Sérgio Manuel and Carpentier, Philippe and Bednář, David and Damborský, Jiří and Marek, Martin},
article_location = {Cambridge},
article_number = {41},
doi = {http://dx.doi.org/10.1039/d0sc03367g},
keywords = {Small-angle scattering; Candida antarctica lipase B},
language = {eng},
issn = {2041-6520},
journal = {Chemical Science},
title = {Decoding the intricate network of molecular interactions of a hyperstable engineered biocatalyst},
url = {https://doi.org/10.1039/D0SC03367G},
volume = {11},
year = {2020}
}
TY - JOUR
ID - 48195
AU - Marková, Klára - Chmelová, Klaudia - Marques, Sérgio Manuel - Carpentier, Philippe - Bednář, David - Damborský, Jiří - Marek, Martin
PY - 2020
TI - Decoding the intricate network of molecular interactions of a hyperstable engineered biocatalyst
JF - Chemical Science
VL - 11
IS - 41
SP - 11162-11178
EP - 11162-11178
PB - Royal Society of Chemistry
SN - 2041-6520
KW - Small-angle scattering
KW - Candida antarctica lipase B
UR - https://doi.org/10.1039/D0SC03367G
N2 - gt; 23 degrees C). An understanding of the structural basis of this hyperstabilization is required in order to develop computer algorithms and predictive tools. Here, we report X-ray structures of DhaA115 at 1.55 angstrom and 1.6 angstrom resolutions and their molecular dynamics trajectories, which unravel the intricate network of interactions that reinforce the aba-sandwich architecture. Unexpectedly, mutations toward bulky aromatic amino acids at the protein surface triggered long-distance (similar to 27 angstrom) backbone changes due to cooperative effects. These cooperative interactions produced an unprecedented double-lock system that: (i) induced backbone changes, (ii) closed the molecular gates to the active site, (iii) reduced the volumes of the main and slot access tunnels, and (iv) occluded the active site. Despite these spatial restrictions, experimental tracing of the access tunnels using krypton derivative crystals demonstrates that transport of ligands is still effective. Our findings highlight key thermostabilization effects and provide a structural basis for designing new thermostable protein catalysts.
ER -
MARKOVÁ, Klára, Klaudia CHMELOVÁ, Sérgio Manuel MARQUES, Philippe CARPENTIER, David BEDNÁŘ, Jiří DAMBORSKÝ a Martin MAREK. Decoding the intricate network of molecular interactions of a hyperstable engineered biocatalyst. \textit{Chemical Science}. Cambridge: Royal Society of Chemistry, 2020, roč.~11, č.~41, s.~11162-11178. ISSN~2041-6520. Dostupné z: https://dx.doi.org/10.1039/d0sc03367g.
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