Structural and Functional Studies of Phosphoenolpyruvate Carboxykinase from Mycobacterium tuberculosis

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F15%3A10319419" target="_blank" >RIV/00216208:11310/15:10319419 - isvavai.cz</a>

Alternative codes found

RIV/61388963:_____/15:00444002

Result on the web

<a href="http://dx.doi.org/10.1371/journal.pone.0120682" target="_blank" >http://dx.doi.org/10.1371/journal.pone.0120682</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1371/journal.pone.0120682" target="_blank" >10.1371/journal.pone.0120682</a>

Result language

angličtina

Original language name

Structural and Functional Studies of Phosphoenolpyruvate Carboxykinase from Mycobacterium tuberculosis

Original language description

Tuberculosis, the second leading infectious disease killer after HIV, remains a top public health priority. The causative agent of tuberculosis, Mycobacterium tuberculosis (Mtb), which can cause both acute and clinically latent infections, reprograms metabolism in response to the host niche. Phosphoenolpyruvate carboxykinase (Pck) is the enzyme at the center of the phosphoenolpyruvate-pyruvate-oxaloacetate node, which is involved in regulating the carbon flow distribution to catabolism, anabolism, or respiration in different states of Mtb infection. Under standard growth conditions, Mtb Pck is associated with gluconeogenesis and catalyzes the metal-dependent formation of phosphoenolpyruvate. In non-replicating Mtb, Pck can catalyze anaplerotic biosynthesis of oxaloacetate. Here, we present insights into the regulation of Mtb Pck activity by divalent cations. Through analysis of the Xray structure of Pck-GDP and Pck-GDP-Mn2+ complexes, mutational analysis of the GDP binding site, and qu

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

CE - Biochemistry

OECD FORD branch

—

Project

<a href="/en/project/LO1302" target="_blank" >LO1302: InterBioMed</a><br>

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2015

Confidentiality

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

Name of the periodical

PLoS ONE

ISSN

1932-6203

e-ISSN

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Volume of the periodical

10

Issue of the periodical within the volume

3

Country of publishing house

US - UNITED STATES

Number of pages

21

Pages from-to

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UT code for WoS article

000351987300164

EID of the result in the Scopus database

2-s2.0-84925740525