ATP synthase from trypanosoma brucei has an elaborated canonical f<inf>1</inf>-domain and conventional catalytic sites

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F18%3A00498761" target="_blank" >RIV/60077344:_____/18:00498761 - isvavai.cz</a>

Result on the web

<a href="http://dx.doi.org/10.1073/pnas.1720940115" target="_blank" >http://dx.doi.org/10.1073/pnas.1720940115</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1073/pnas.1720940115" target="_blank" >10.1073/pnas.1720940115</a>

Result language

angličtina

Original language name

ATP synthase from trypanosoma brucei has an elaborated canonical f<inf>1</inf>-domain and conventional catalytic sites

Original language description

The structures and functions of the components of ATP synthases, especially those subunits involved directly in the catalytic formation of ATP, are widely conserved in metazoans, fungi, eubacteria, and plant chloroplasts. On the basis of a map at 32.5-Å resolution determined in situ in the mitochondria of Trypanosoma brucei by electron cryotomography, it has been proposed that the ATP synthase in this species has a noncanonical structure and different catalytic sites in which the catalytically essential arginine finger is provided not by the α-subunit adjacent to the catalytic nucleotide-binding site as in all species investigated to date, but rather by a protein, p18, found only in the euglenozoa. A crystal structure at 3.2-Å resolution of the catalytic domain of the same enzyme demonstrates that this proposal is incorrect. In many respects, the structure is similar to the structures of F1- ATPases determined previously. The α3β3-spherical portion of the catalytic domain in which the three catalytic sites are found, plus the central stalk, are highly conserved, and the arginine finger is provided conventionally by the α-subunits adjacent to each of the three catalytic sites found in the β-subunits. Thus, the enzyme has a conventional catalytic mechanism. The structure differs from previous described structures by the presence of a p18 subunit, identified only in the euglenozoa, associated with the external surface of each of the three α-subunits, thereby elaborating the F1-domain. Subunit p18 is a pentatricopeptide repeat (PPR) protein with three PPRs and appears to have no function in the catalytic mechanism of the enzyme.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

30405 - Medical biotechnology related ethics

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2018

Confidentiality

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

Name of the periodical

Proceedings of the National Academy of Sciences of the United States of America

ISSN

0027-8424

e-ISSN

—

Volume of the periodical

115

Issue of the periodical within the volume

9

Country of publishing house

US - UNITED STATES

Number of pages

6

Pages from-to

2102-2107

UT code for WoS article

000426152500060

EID of the result in the Scopus database

2-s2.0-85042686020