Molecular dynamics comparison of E. coli WrbA apoprotein and holoprotein

Result code in 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>

Alternative codes found

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

Result on the web

<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>

Result language

angličtina

Original language name

Molecular dynamics comparison of E. coli WrbA apoprotein and holoprotein

Original language description

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

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EH - Ecology - communities

OECD FORD branch

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Project

<a href="/en/project/GAP207%2F10%2F1934" target="_blank" >GAP207/10/1934: Structural insight into E. coli protein WrbA, the founding member of a family of proteins implicated in defense of cells against oxidative stress</a><br>

Continuities

S - Specificky vyzkum na vysokych skolach<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

Name of the periodical

Journal of Molecular Modeling

ISSN

1610-2940

e-ISSN

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Volume of the periodical

20

Issue of the periodical within the volume

9

Country of publishing house

DE - GERMANY

Number of pages

14

Pages from-to

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UT code for WoS article

000341865300006

EID of the result in the Scopus database

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