1.2 angstrom resolution crystal structure of Escherichia coli WrbA holoprotein

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F13%3A10191657" target="_blank" >RIV/00216208:11310/13:10191657 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60076658:12310/13:43885620 RIV/60076658:12520/13:43885620

Výsledek na webu

<a href="http://dx.doi.org/10.1107/S0907444913017162" target="_blank" >http://dx.doi.org/10.1107/S0907444913017162</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1107/S0907444913017162" target="_blank" >10.1107/S0907444913017162</a>

Jazyk výsledku

angličtina

Název v původním jazyce

1.2 angstrom resolution crystal structure of Escherichia coli WrbA holoprotein

Popis výsledku v původním jazyce

The Escherichia coli protein WrbA, an FMN-dependent NAD(P)H:quinone oxidoreductase, was crystallized under new conditions in the presence of FAD or the native cofactor FMN. Slow-growing deep yellow crystals formed with FAD display the tetragonal bipyramidal shape typical for WrbA and diffract to 1.2 angstrom resolution, the highest yet reported. Faster-growing deep yellow crystals formed with FMN display an atypical shape, but diffract to only similar to 1.6 angstrom resolution and are not analysed further here. The 1.2 angstrom resolution structure detailed here revealed only FMN in the active site and no electron density that can accommodate the missing parts of FAD. The very high resolution supports the modelling of the FMN isoalloxazine with a small but distinct propeller twist, apparently the first experimental observation of this predicted conformation, which appears to be enforced by the protein through a network of hydrogen bonds. Comparison of the electron density of the twist

Název v anglickém jazyce

1.2 angstrom resolution crystal structure of Escherichia coli WrbA holoprotein

Popis výsledku anglicky

The Escherichia coli protein WrbA, an FMN-dependent NAD(P)H:quinone oxidoreductase, was crystallized under new conditions in the presence of FAD or the native cofactor FMN. Slow-growing deep yellow crystals formed with FAD display the tetragonal bipyramidal shape typical for WrbA and diffract to 1.2 angstrom resolution, the highest yet reported. Faster-growing deep yellow crystals formed with FMN display an atypical shape, but diffract to only similar to 1.6 angstrom resolution and are not analysed further here. The 1.2 angstrom resolution structure detailed here revealed only FMN in the active site and no electron density that can accommodate the missing parts of FAD. The very high resolution supports the modelling of the FMN isoalloxazine with a small but distinct propeller twist, apparently the first experimental observation of this predicted conformation, which appears to be enforced by the protein through a network of hydrogen bonds. Comparison of the electron density of the twist

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/ME09016" target="_blank" >ME09016: Úloha proteinu WrbA v životě</a><br>

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

Acta Crystallographica Section D: Biological Crystallography

ISSN

0907-4449

e-ISSN

—

Svazek periodika

69

Číslo periodika v rámci svazku

9

Stát vydavatele periodika

FR - Francouzská republika

Počet stran výsledku

10

Strana od-do

1748-1757

Kód UT WoS článku

000324818000012

EID výsledku v databázi Scopus

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