-
Something wrong with this record ?
ATP synthase from Trypanosoma brucei has an elaborated canonical F1-domain and conventional catalytic sites
MG. Montgomery, O. Gahura, AGW. Leslie, A. Zíková, JE. Walker,
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
NLK
Free Medical Journals
from 1915 to 6 months ago
Freely Accessible Science Journals
from 1915 to 6 months ago
PubMed Central
from 1915 to 6 months ago
Europe PubMed Central
from 1915 to 6 months ago
Open Access Digital Library
from 1915-01-01
Open Access Digital Library
from 1915-01-15
- MeSH
- Catalytic Domain MeSH
- Protein Conformation MeSH
- Mitochondrial Proton-Translocating ATPases genetics metabolism MeSH
- Models, Molecular MeSH
- Protein Subunits MeSH
- Protozoan Proteins genetics metabolism MeSH
- Gene Expression Regulation, Enzymologic MeSH
- Trypanosoma brucei brucei enzymology genetics MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
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.
References provided by Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc18033318
- 003
- CZ-PrNML
- 005
- 20181010125507.0
- 007
- ta
- 008
- 181008s2018 xxu f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.1073/pnas.1720940115 $2 doi
- 035 __
- $a (PubMed)29440423
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a xxu
- 100 1_
- $a Montgomery, Martin G $u The Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, United Kingdom.
- 245 10
- $a ATP synthase from Trypanosoma brucei has an elaborated canonical F1-domain and conventional catalytic sites / $c MG. Montgomery, O. Gahura, AGW. Leslie, A. Zíková, JE. Walker,
- 520 9_
- $a 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.
- 650 _2
- $a katalytická doména $7 D020134
- 650 _2
- $a regulace genové exprese enzymů $7 D015971
- 650 _2
- $a mitochondriální protonové ATPasy $x genetika $x metabolismus $7 D025261
- 650 _2
- $a molekulární modely $7 D008958
- 650 _2
- $a konformace proteinů $7 D011487
- 650 _2
- $a podjednotky proteinů $7 D021122
- 650 _2
- $a protozoální proteiny $x genetika $x metabolismus $7 D015800
- 650 _2
- $a Trypanosoma brucei brucei $x enzymologie $x genetika $7 D014346
- 655 _2
- $a časopisecké články $7 D016428
- 655 _2
- $a práce podpořená grantem $7 D013485
- 700 1_
- $a Gahura, Ondřej $u The Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, United Kingdom. Institute of Parasitology, Biology Centre, Czech Academy of Sciences, 37005 České Budějovice, Czech Republic.
- 700 1_
- $a Leslie, Andrew G W $u The Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom.
- 700 1_
- $a Zíková, Alena $u Institute of Parasitology, Biology Centre, Czech Academy of Sciences, 37005 České Budějovice, Czech Republic.
- 700 1_
- $a Walker, John E $u The Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, United Kingdom; walker@mrc-mbu.cam.ac.uk.
- 773 0_
- $w MED00010472 $t Proceedings of the National Academy of Sciences of the United States of America $x 1091-6490 $g Roč. 115, č. 9 (2018), s. 2102-2107
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/29440423 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y a $z 0
- 990 __
- $a 20181008 $b ABA008
- 991 __
- $a 20181010125956 $b ABA008
- 999 __
- $a ok $b bmc $g 1340879 $s 1030312
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2018 $b 115 $c 9 $d 2102-2107 $e 20180212 $i 1091-6490 $m Proceedings of the National Academy of Sciences of the United States of America $n Proc Natl Acad Sci U S A $x MED00010472
- LZP __
- $a Pubmed-20181008
