Structure-function studies of the G-domain from human gem, a novel small G-protein

Yarden Opatowsky; Yehezkel Sasson; Isabella Shaked; Yvona Ward; Orna Chomsky-Hecht; Yael Litvak; Zvi Selinger; Kathleen Kelly; Joel A. Hirsch

doi:10.1016/j.febslet.2006.09.067

Structure-function studies of the G-domain from human gem, a novel small G-protein

Yarden Opatowsky, Yehezkel Sasson, Isabella Shaked, Yvona Ward, Orna Chomsky-Hecht, Yael Litvak, Zvi Selinger, Kathleen Kelly, Joel A. Hirsch^*

^*Corresponding author for this work

Department of Biological Chemistry

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

25 Scopus citations

Abstract

Gem, a member of the Rad,Gem/Kir subfamily of small G-proteins, has unique sequence features. We report here the crystallographic structure determination of the Gem G-domain in complex with nucleotide to 2.4 Å resolution. Although the basic Ras protein fold is maintained, the Gem switch regions emphatically differ from the Ras paradigm. Our ensuing biochemical characterization indicates that Gem G-domain markedly prefers GDP over GTP. Two known functions of Gem are distinctly affected by spatially separated clusters of mutations.

Original language	English
Pages (from-to)	5959-5964
Number of pages	6
Journal	FEBS Letters
Volume	580
Issue number	25
DOIs	https://doi.org/10.1016/j.febslet.2006.09.067
State	Published - 30 Oct 2006

Bibliographical note

Funding Information:
Thanks go to the staff of ID14-4 (ESRF, France) for assistance with diffraction experiments. We thank Doug Andres for generously sharing Cav β expression constructs. Preliminary studies were supported by a grant from the US–Israel Binational Science Foundation (JAH, KK). Continuing work has been funded by a grant to JAH from the Israel Cancer Research Fund and by NIH grant EY 03529 to ZS. Appendix A

Keywords

Calcium channel
Crystallography
Cytoskeleton
G-protein
Nucleotide

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10.1016/j.febslet.2006.09.067

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title = "Structure-function studies of the G-domain from human gem, a novel small G-protein",

abstract = "Gem, a member of the Rad,Gem/Kir subfamily of small G-proteins, has unique sequence features. We report here the crystallographic structure determination of the Gem G-domain in complex with nucleotide to 2.4 {\AA} resolution. Although the basic Ras protein fold is maintained, the Gem switch regions emphatically differ from the Ras paradigm. Our ensuing biochemical characterization indicates that Gem G-domain markedly prefers GDP over GTP. Two known functions of Gem are distinctly affected by spatially separated clusters of mutations.",

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author = "Yarden Opatowsky and Yehezkel Sasson and Isabella Shaked and Yvona Ward and Orna Chomsky-Hecht and Yael Litvak and Zvi Selinger and Kathleen Kelly and Hirsch, {Joel A.}",

note = "Funding Information: Thanks go to the staff of ID14-4 (ESRF, France) for assistance with diffraction experiments. We thank Doug Andres for generously sharing Cav β expression constructs. Preliminary studies were supported by a grant from the US–Israel Binational Science Foundation (JAH, KK). Continuing work has been funded by a grant to JAH from the Israel Cancer Research Fund and by NIH grant EY 03529 to ZS. Appendix A ",

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AU - Opatowsky, Yarden

AU - Sasson, Yehezkel

AU - Shaked, Isabella

AU - Ward, Yvona

AU - Chomsky-Hecht, Orna

AU - Litvak, Yael

AU - Selinger, Zvi

AU - Kelly, Kathleen

AU - Hirsch, Joel A.

N1 - Funding Information: Thanks go to the staff of ID14-4 (ESRF, France) for assistance with diffraction experiments. We thank Doug Andres for generously sharing Cav β expression constructs. Preliminary studies were supported by a grant from the US–Israel Binational Science Foundation (JAH, KK). Continuing work has been funded by a grant to JAH from the Israel Cancer Research Fund and by NIH grant EY 03529 to ZS. Appendix A

PY - 2006/10/30

Y1 - 2006/10/30

N2 - Gem, a member of the Rad,Gem/Kir subfamily of small G-proteins, has unique sequence features. We report here the crystallographic structure determination of the Gem G-domain in complex with nucleotide to 2.4 Å resolution. Although the basic Ras protein fold is maintained, the Gem switch regions emphatically differ from the Ras paradigm. Our ensuing biochemical characterization indicates that Gem G-domain markedly prefers GDP over GTP. Two known functions of Gem are distinctly affected by spatially separated clusters of mutations.

AB - Gem, a member of the Rad,Gem/Kir subfamily of small G-proteins, has unique sequence features. We report here the crystallographic structure determination of the Gem G-domain in complex with nucleotide to 2.4 Å resolution. Although the basic Ras protein fold is maintained, the Gem switch regions emphatically differ from the Ras paradigm. Our ensuing biochemical characterization indicates that Gem G-domain markedly prefers GDP over GTP. Two known functions of Gem are distinctly affected by spatially separated clusters of mutations.

KW - Calcium channel

KW - Crystallography

KW - Cytoskeleton

KW - G-protein

KW - Nucleotide

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JO - FEBS Letters

JF - FEBS Letters

IS - 25

ER -

Structure-function studies of the G-domain from human gem, a novel small G-protein

Abstract

Bibliographical note

Keywords

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