A Computational Study of the Glycine-Rich Loop of Mitochondrial Processing Peptidase

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F13%3A10191950" target="_blank" >RIV/00216208:11310/13:10191950 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/13:00423430 RIV/61989592:15310/13:33148395

Výsledek na webu

<a href="http://dx.doi.org/10.1371/journal.pone.0074518" target="_blank" >http://dx.doi.org/10.1371/journal.pone.0074518</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1371/journal.pone.0074518" target="_blank" >10.1371/journal.pone.0074518</a>

Jazyk výsledku

angličtina

Název v původním jazyce

A Computational Study of the Glycine-Rich Loop of Mitochondrial Processing Peptidase

Popis výsledku v původním jazyce

An all atomic, non-restrained molecular dynamics (MD) simulation in explicit water was used to study in detail the structural features of the highly conserved glycine-rich loop (GRL) of the a-subunit of the yeast mitochondrial processing peptidase (MPP)and its importance for the tertiary and quaternary conformation of MPP. Wild-type and GRL-deleted MPP structures were studied using non-restrained MD simulations, both in the presence and the absence of a substrate in the peptidase active site. TargetedMD simulations were employed to study the mechanism of substrate translocation from the GRL to the active site. We demonstrate that the natural conformational flexibility of the GRL is crucial for the substrate translocation process from outside the enzyme towards the MPP active site. We show that the a-helical conformation of the substrate is important not only during its initial interaction with MPP (i.e. substrate recognition), but also later, at least during the first third of the su

Název v anglickém jazyce

A Computational Study of the Glycine-Rich Loop of Mitochondrial Processing Peptidase

Popis výsledku anglicky

An all atomic, non-restrained molecular dynamics (MD) simulation in explicit water was used to study in detail the structural features of the highly conserved glycine-rich loop (GRL) of the a-subunit of the yeast mitochondrial processing peptidase (MPP)and its importance for the tertiary and quaternary conformation of MPP. Wild-type and GRL-deleted MPP structures were studied using non-restrained MD simulations, both in the presence and the absence of a substrate in the peptidase active site. TargetedMD simulations were employed to study the mechanism of substrate translocation from the GRL to the active site. We demonstrate that the natural conformational flexibility of the GRL is crucial for the substrate translocation process from outside the enzyme towards the MPP active site. We show that the a-helical conformation of the substrate is important not only during its initial interaction with MPP (i.e. substrate recognition), but also later, at least during the first third of the su

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2013

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

PLoS ONE

ISSN

1932-6203

e-ISSN

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Svazek periodika

8

Číslo periodika v rámci svazku

9

Stát vydavatele periodika

ES - Španělské království

Počet stran výsledku

13

Strana od-do

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Kód UT WoS článku

000324408400082

EID výsledku v databázi Scopus

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