Crystallization and preliminary X-ray diffraction studies of Drosophila melanogaster Gαo-subunit of heterotrimeric G protein in complex with the RGS domain of CG5036

Svetlana Tishchenko; Azat Gabdulkhakov; Uliana Tin; Olga Kostareva; Chen Lin; Vladimir L. Katanaev

doi:10.1107/S174430911204804X

Crystallization and preliminary X-ray diffraction studies of Drosophila melanogaster Gαo-subunit of heterotrimeric G protein in complex with the RGS domain of CG5036

Svetlana Tishchenko^*, Azat Gabdulkhakov, Uliana Tin, Olga Kostareva, Chen Lin, Vladimir L. Katanaev

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

4 Citations (Scopus)

Abstract

Regulator of G-protein signalling (RGS) proteins negatively regulate heterotrimeric G-protein signalling through their conserved RGS domains. RGS domains act as GTPase-activating proteins, accelerating the GTP hydrolysis rate of the activated form of Gα-subunits. Although omnipresent in eukaryotes, RGS proteins have not been adequately analysed in non-mammalian organisms. The Drosophila melanogaster Gαo-subunit and the RGS domain of its interacting partner CG5036 have been overproduced and purified; the crystallization of the complex of the two proteins using PEG 4000 as a crystallizing agent and preliminary X-ray crystallographic analysis are reported. Diffraction data were collected to 2.0 Å resolution using a synchrotron-radiation source.

Original language	English
Pages (from-to)	61-64
Number of pages	4
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	69
Issue number	1
DOIs	https://doi.org/10.1107/S174430911204804X
Publication status	Published - Jan 2013
Externally published	Yes

Keywords

Drosophila melanogaster
Gαo-subunit
G-protein signalling

Access to Document

10.1107/S174430911204804X

Cite this

Tishchenko, S., Gabdulkhakov, A., Tin, U., Kostareva, O., Lin, C., & Katanaev, V. L. (2013). Crystallization and preliminary X-ray diffraction studies of Drosophila melanogaster Gαo-subunit of heterotrimeric G protein in complex with the RGS domain of CG5036. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 69(1), 61-64. https://doi.org/10.1107/S174430911204804X

@article{1cbab1b123c64ef1ba3306ce7b4c4dc9,

title = "Crystallization and preliminary X-ray diffraction studies of Drosophila melanogaster Gαo-subunit of heterotrimeric G protein in complex with the RGS domain of CG5036",

abstract = "Regulator of G-protein signalling (RGS) proteins negatively regulate heterotrimeric G-protein signalling through their conserved RGS domains. RGS domains act as GTPase-activating proteins, accelerating the GTP hydrolysis rate of the activated form of Gα-subunits. Although omnipresent in eukaryotes, RGS proteins have not been adequately analysed in non-mammalian organisms. The Drosophila melanogaster Gαo-subunit and the RGS domain of its interacting partner CG5036 have been overproduced and purified; the crystallization of the complex of the two proteins using PEG 4000 as a crystallizing agent and preliminary X-ray crystallographic analysis are reported. Diffraction data were collected to 2.0 {\AA} resolution using a synchrotron-radiation source.",

keywords = "Drosophila melanogaster, Gαo-subunit, G-protein signalling",

author = "Svetlana Tishchenko and Azat Gabdulkhakov and Uliana Tin and Olga Kostareva and Chen Lin and Katanaev, {Vladimir L.}",

year = "2013",

month = jan,

doi = "10.1107/S174430911204804X",

language = "English",

volume = "69",

pages = "61--64",

journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

issn = "1744-3091",

publisher = "John Wiley and Sons Ltd",

number = "1",

}

Tishchenko, S, Gabdulkhakov, A, Tin, U, Kostareva, O, Lin, C & Katanaev, VL 2013, 'Crystallization and preliminary X-ray diffraction studies of Drosophila melanogaster Gαo-subunit of heterotrimeric G protein in complex with the RGS domain of CG5036', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 69, no. 1, pp. 61-64. https://doi.org/10.1107/S174430911204804X

Crystallization and preliminary X-ray diffraction studies of Drosophila melanogaster Gαo-subunit of heterotrimeric G protein in complex with the RGS domain of CG5036. / Tishchenko, Svetlana; Gabdulkhakov, Azat; Tin, Uliana et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 69, No. 1, 01.2013, p. 61-64.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Crystallization and preliminary X-ray diffraction studies of Drosophila melanogaster Gαo-subunit of heterotrimeric G protein in complex with the RGS domain of CG5036

AU - Tishchenko, Svetlana

AU - Gabdulkhakov, Azat

AU - Tin, Uliana

AU - Kostareva, Olga

AU - Lin, Chen

AU - Katanaev, Vladimir L.

PY - 2013/1

Y1 - 2013/1

N2 - Regulator of G-protein signalling (RGS) proteins negatively regulate heterotrimeric G-protein signalling through their conserved RGS domains. RGS domains act as GTPase-activating proteins, accelerating the GTP hydrolysis rate of the activated form of Gα-subunits. Although omnipresent in eukaryotes, RGS proteins have not been adequately analysed in non-mammalian organisms. The Drosophila melanogaster Gαo-subunit and the RGS domain of its interacting partner CG5036 have been overproduced and purified; the crystallization of the complex of the two proteins using PEG 4000 as a crystallizing agent and preliminary X-ray crystallographic analysis are reported. Diffraction data were collected to 2.0 Å resolution using a synchrotron-radiation source.

AB - Regulator of G-protein signalling (RGS) proteins negatively regulate heterotrimeric G-protein signalling through their conserved RGS domains. RGS domains act as GTPase-activating proteins, accelerating the GTP hydrolysis rate of the activated form of Gα-subunits. Although omnipresent in eukaryotes, RGS proteins have not been adequately analysed in non-mammalian organisms. The Drosophila melanogaster Gαo-subunit and the RGS domain of its interacting partner CG5036 have been overproduced and purified; the crystallization of the complex of the two proteins using PEG 4000 as a crystallizing agent and preliminary X-ray crystallographic analysis are reported. Diffraction data were collected to 2.0 Å resolution using a synchrotron-radiation source.

KW - Drosophila melanogaster

KW - Gαo-subunit

KW - G-protein signalling

UR - http://www.scopus.com/inward/record.url?scp=84872110863&partnerID=8YFLogxK

U2 - 10.1107/S174430911204804X

DO - 10.1107/S174430911204804X

M3 - Article

C2 - 23295489

AN - SCOPUS:84872110863

SN - 1744-3091

VL - 69

SP - 61

EP - 64

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

IS - 1

ER -

Tishchenko S, Gabdulkhakov A, Tin U, Kostareva O, Lin C, Katanaev VL. Crystallization and preliminary X-ray diffraction studies of Drosophila melanogaster Gαo-subunit of heterotrimeric G protein in complex with the RGS domain of CG5036. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2013 Jan;69(1):61-64. doi: 10.1107/S174430911204804X

Crystallization and preliminary X-ray diffraction studies of Drosophila melanogaster Gαo-subunit of heterotrimeric G protein in complex with the RGS domain of CG5036

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this