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

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Holoenzyme structures of endothelial nitric oxide synthase - An allosteric role for calmodulin in pivoting the FMN domain for electron transfer Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
rdfs:seeAlso	http://dx.doi.org/10.1016/j.jsb.2014.08.006
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 the opposite 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 indicate that 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 homodimer of eNOS. (C) 2014 Elsevier Inc. All rights reserved. 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 the opposite 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 indicate that 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 homodimer of eNOS. (C) 2014 Elsevier Inc. All rights reserved. (en)
Title	Holoenzyme structures of endothelial nitric oxide synthase - An allosteric role for calmodulin in pivoting the FMN domain for electron transfer Holoenzyme structures of endothelial nitric oxide synthase - An allosteric role for calmodulin in pivoting the FMN domain for electron transfer (en)
skos:prefLabel	Holoenzyme structures of endothelial nitric oxide synthase - An allosteric role for calmodulin in pivoting the FMN domain for electron transfer Holoenzyme structures of endothelial nitric oxide synthase - An allosteric role for calmodulin in pivoting the FMN domain for electron transfer (en)
skos:notation	RIV/00216208:11110/14:10283778!RIV15-MSM-11110___
http://linked.open...avai/riv/aktivita	I P
http://linked.open...avai/riv/aktivity	I, P(ED1.1.00/02.0109)
http://linked.open...iv/cisloPeriodika	1
http://linked.open...vai/riv/dodaniDat	2015
http://linked.open...aciTvurceVysledku	Martásek, Pavel
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Univerzita Karlova v Praze / 1. lékařská fakulta
http://linked.open...dnocenehoVysledku	19631
http://linked.open...ai/riv/idVysledku	RIV/00216208:11110/14:10283778
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Image processing; Electron transfer; Nitric oxide synthase; Three-dimensional reconstruction; Electron cryomicroscopy; Calmodulin (en)
http://linked.open.../riv/klicoveSlovo	Image processing Nitric oxide synthase Electron transfer Calmodulin Electron cryomicroscopy Three-dimensional reconstruction
http://linked.open...odStatuVydavatele	US - Spojené státy americké
http://linked.open...ontrolniKodProRIV	[25306C9FAF70]
http://linked.open...i/riv/nazevZdroje	Journal of Structural Biology
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	1 (xsd:int)
http://linked.open...cetTvurcuVysledku	8 (xsd:int)
http://linked.open...vavai/riv/projekt	Biotechnology and Biomedicine Centre of the Academy of Sciences and Charles University
http://linked.open...UplatneniVysledku	2014
http://linked.open...v/svazekPeriodika	188
http://linked.open...iv/tvurceVysledku	Martásek, Pavel Roman, Linda J. Hanein, Dorit Masters, Bettie Sue Page, Christopher Swift, Mark Volkmann, Niels Xu, Xiao-Ping
http://linked.open...ain/vavai/riv/wos	000343354300006
issn	1047-8477
number of pages	9 (xsd:int)
http://bibframe.org/vocab/doi	10.1016/j.jsb.2014.08.006
http://localhost/t...ganizacniJednotka	11110

Faceted Search & Find service v1.16.118 as of Jun 21 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 48 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software