1.2 angstrom resolution crystal structure of Escherichia coli WrbA holoprotein
The result's identifiers
Result code in 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>
Alternative codes found
RIV/60076658:12310/13:43885620 RIV/60076658:12520/13:43885620
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
1.2 angstrom resolution crystal structure of Escherichia coli WrbA holoprotein
Original language description
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
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/ME09016" target="_blank" >ME09016: The role of WrbA protein in life</a><br>
Continuities
S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Acta Crystallographica Section D: Biological Crystallography
ISSN
0907-4449
e-ISSN
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Volume of the periodical
69
Issue of the periodical within the volume
9
Country of publishing house
FR - FRANCE
Number of pages
10
Pages from-to
1748-1757
UT code for WoS article
000324818000012
EID of the result in the Scopus database
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