The chromatin remodeler SMARCA5 binds to d-block metal supports: Characterization of affinities by IMAC chromatography and QM analysis
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378041%3A_____%2F24%3A00599711" target="_blank" >RIV/68378041:_____/24:00599711 - isvavai.cz</a>
Alternative codes found
RIV/86652036:_____/24:00599711 RIV/00216208:11110/24:10488272
Result on the web
<a href="https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0309134" target="_blank" >https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0309134</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1371/journal.pone.0309134" target="_blank" >10.1371/journal.pone.0309134</a>
Alternative languages
Result language
angličtina
Original language name
The chromatin remodeler SMARCA5 binds to d-block metal supports: Characterization of affinities by IMAC chromatography and QM analysis
Original language description
The ISWI family protein SMARCA5 contains the ATP-binding pocket that coordinates the catalytic Mg2+ ion and water molecules for ATP hydrolysis. In this study, we demonstrate that SMARCA5 can also possess an alternative metal-binding ability. First, we isolated SMARCA5 on the cobalt column (IMAC) to near homogeneity. Examination of the interactions of SMARCA5 with metal-chelating supports showed that, apart from Co2+, it binds to Cu2+, Zn2+ and Ni2+. The efficiency of the binding to the last-listed metal was influenced by the chelating ligand, resulting in a strong preference for Ni-NTA over the Ni-CM-Asp equivalent. To gain insight in the preferential affinity for the Ni-NTA ligand, QM calculations were performed on model systems and metal-ligand complexes with a limited protein fragment of SMARCA5 containing the double-histidine (dHis) motif. The calculations correlated the observed affinity with the relative stability of the d-block metals to tetradentate ligand coordination over tridentate, as well as their overall octahedral coordination capacity. Likewise, binding free energies derived from model imidazole complexes mirrored the observed Ni-NTA/Ni-CM-Asp preferential affinity. Finally, similar calculations on complexes with a SMARCA5 peptide fragment derived from the AlphaFold structural prediction, captured almost accurately the expected relative stability of the TM complexes, and produced a large energetic separation (similar to 10 kcal center dot mol(-1)) between Ni-NTA and Ni-CM-Asp in favour of the former.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2024
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
PLoS ONE
ISSN
1932-6203
e-ISSN
1932-6203
Volume of the periodical
19
Issue of the periodical within the volume
10
Country of publishing house
US - UNITED STATES
Number of pages
21
Pages from-to
e0309134
UT code for WoS article
001330415500002
EID of the result in the Scopus database
2-s2.0-85205756390