Molecular dynamics comparison of E. coli WrbA apoprotein and holoprotein

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F14%3A10288320" target="_blank" >RIV/00216208:11310/14:10288320 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/67179843:_____/14:00437116 RIV/61388971:_____/14:00437116 RIV/60076658:12310/14:43887251

Výsledek na webu

<a href="http://dx.doi.org/10.1007/s00894-014-2400-8" target="_blank" >http://dx.doi.org/10.1007/s00894-014-2400-8</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00894-014-2400-8" target="_blank" >10.1007/s00894-014-2400-8</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Molecular dynamics comparison of E. coli WrbA apoprotein and holoprotein

Popis výsledku v původním jazyce

WrbA is a novel multimeric flavodoxin-like protein of unknown function. A recent high-resolution X-ray crystal structure of E. coli WrbA holoprotein revealed a methionine sulfoxide residue with full occupancy in the FMN-binding site, a finding that was confirmed by mass spectrometry. In an effort to evaluate whether methionine sulfoxide may have a role in WrbA function, the present analyses were undertaken using molecular dynamics simulations in combination with further mass spectrometry of the protein.Methionine sulfoxide formation upon reconstitution of purified apoWrbA with oxidized FMN is fast as judged by kinetic mass spectrometry, being complete in similar to 5 h and resulting in complete conversion at the active-site methionine with minor extents of conversion at heterogeneous second sites. Analysis of methionine oxidation states during purification of holoWrbA from bacterial cells reveals that methionine is not oxidized prior to reconstitution, indicating that methionine sulfo

Název v anglickém jazyce

Molecular dynamics comparison of E. coli WrbA apoprotein and holoprotein

Popis výsledku anglicky

WrbA is a novel multimeric flavodoxin-like protein of unknown function. A recent high-resolution X-ray crystal structure of E. coli WrbA holoprotein revealed a methionine sulfoxide residue with full occupancy in the FMN-binding site, a finding that was confirmed by mass spectrometry. In an effort to evaluate whether methionine sulfoxide may have a role in WrbA function, the present analyses were undertaken using molecular dynamics simulations in combination with further mass spectrometry of the protein.Methionine sulfoxide formation upon reconstitution of purified apoWrbA with oxidized FMN is fast as judged by kinetic mass spectrometry, being complete in similar to 5 h and resulting in complete conversion at the active-site methionine with minor extents of conversion at heterogeneous second sites. Analysis of methionine oxidation states during purification of holoWrbA from bacterial cells reveals that methionine is not oxidized prior to reconstitution, indicating that methionine sulfo

Druh

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

CEP obor

EH - Ekologie – společenstva

OECD FORD obor

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Projekt

<a href="/cs/project/GAP207%2F10%2F1934" target="_blank" >GAP207/10/1934: Strukturní pohled na funkci proteinu WrbA – zakládající člen rodiny proteinů zahrnutých v buněčné obraně proti oxidativnímu stresu.</a><br>

Návaznosti

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

Rok uplatnění

2014

Kód důvěrnosti údajů

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

Název periodika

Journal of Molecular Modeling

ISSN

1610-2940

e-ISSN

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Svazek periodika

20

Číslo periodika v rámci svazku

9

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

14

Strana od-do

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Kód UT WoS článku

000341865300006

EID výsledku v databázi Scopus

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