Phosphate binding in the active centre of tomato multifunctional nuclease TBN1 and analysis of superhelix formation by the enzyme

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F15%3A43899762" target="_blank" >RIV/60461373:22330/15:43899762 - isvavai.cz</a>

Výsledek na webu

<a href="http://scripts.iucr.org/cgi-bin/paper?S2053230X15018324" target="_blank" >http://scripts.iucr.org/cgi-bin/paper?S2053230X15018324</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1107/S2053230X15018324" target="_blank" >10.1107/S2053230X15018324</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Phosphate binding in the active centre of tomato multifunctional nuclease TBN1 and analysis of superhelix formation by the enzyme

Popis výsledku v původním jazyce

Tomato multifunctional nuclease TBN1 belongs to the type I nuclease family, which plays an important role in apoptotic processes and cell senescence in plants. The newly solved structure of the N211D mutant is reported. Although the main crystal-packingmotif (the formation of superhelices) is conserved, the details differ among the known structures. A phosphate ion was localized in the active site of the enzyme. The binding of the surface loop to the active centre is stabilized by the phosphate ion, which correlates with the observed aggregation of TBN1 in phosphate buffer. The conserved binding of the surface loop to the active centre suggests biological relevance of the contact in a regulatory function or in the formation of oligomers.

Název v anglickém jazyce

Phosphate binding in the active centre of tomato multifunctional nuclease TBN1 and analysis of superhelix formation by the enzyme

Popis výsledku anglicky

Tomato multifunctional nuclease TBN1 belongs to the type I nuclease family, which plays an important role in apoptotic processes and cell senescence in plants. The newly solved structure of the N211D mutant is reported. Although the main crystal-packingmotif (the formation of superhelices) is conserved, the details differ among the known structures. A phosphate ion was localized in the active site of the enzyme. The binding of the surface loop to the active centre is stabilized by the phosphate ion, which correlates with the observed aggregation of TBN1 in phosphate buffer. The conserved binding of the surface loop to the active centre suggests biological relevance of the contact in a regulatory function or in the formation of oligomers.

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

Acta Crystallographica Section F-Structural Biology and Crystallization Communications

ISSN

1744-3091

e-ISSN

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Svazek periodika

71

Číslo periodika v rámci svazku

1.11.2015

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

8

Strana od-do

1408-1415

Kód UT WoS článku

000364557700008

EID výsledku v databázi Scopus

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