Holoenzyme structures of endothelial nitric oxide synthase - An allosteric role for calmodulin in pivoting the FMN domain for electron transfer

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11110%2F14%3A10283778" target="_blank" >RIV/00216208:11110/14:10283778 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1016/j.jsb.2014.08.006" target="_blank" >http://dx.doi.org/10.1016/j.jsb.2014.08.006</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.jsb.2014.08.006" target="_blank" >10.1016/j.jsb.2014.08.006</a>

Result language
angličtina
Original language name
Holoenzyme structures of endothelial nitric oxide synthase - An allosteric role for calmodulin in pivoting the FMN domain for electron transfer
Original language description
While the three-dimensional structures of heme- and flavin-binding domains of the NOS isoforms have been determined, the structures of the holoenzymes remained elusive. Application of electron cryo-microscopy and structural modeling of the bovine endothelial nitric oxide synthase (eNOS) holoenzyme produced detailed models of the intact holoenzyme in the presence and absence of Ca2+/calmodulin (CaM). These models accommodate the cross-electron transfer from the reductase in one monomer to the heme in theopposite monomer. The heme domain acts as the anchoring dimeric structure for the entire enzyme molecule, while the FMN domain is activated by CaM to move flexibly to bridge the distance between the reductase and oxygenase domains. Our results indicatethat the key regulatory role of CaM involves the stabilization of structural intermediates and precise positioning of the pivot for the FMN domain tethered shuttling motion to accommodate efficient and rapid electron transfer in the homod
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Project
<a href="/en/project/ED1.1.00%2F02.0109" target="_blank" >ED1.1.00/02.0109: Biotechnology and Biomedicine Centre of the Academy of Sciences and Charles University</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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