Domain arrangement of Der, a switch protein containing two GTPase domains

Victoria L. Robinson; Jihwan Hwang; Eileen Fox; Masayori Inouye; Ann M. Stock

doi:https://doi.org/10.1016/S0969-2126(02)00905-X

Domain arrangement of Der, a switch protein containing two GTPase domains

Victoria L. Robinson, Jihwan Hwang, Eileen Fox, Masayori Inouye, Ann M. Stock

Rutgers, The State University

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

57 Scopus citations

Abstract

The EngA subfamily of essential bacterial GTPases has a unique domain structure consisting of two adjacent GTPase domains (GD1 and GD2) and a C-terminal domain. The structure of Thermotoga maritima Der bound to GDP determined at 1.9 Å resolution reveals a novel domain arrangement in which the GTPase domains pack at either side of the C-terminal domain. Unexpectedly, the C-terminal domain resembles a KH domain, missing the distinctive RNA recognition elements. Conserved motifs of the nucleotide binding site of GD1 are integral parts of the GD1-KH domain interface, suggesting the interactions between these two domains are directly influenced by the GTP/GDP cycling of the protein. In contrast, the GD2-KH domain interface is distal to the GDP binding site of GD2.

Original language	English (US)
Pages (from-to)	1649-1658
Number of pages	10
Journal	Structure
Volume	10
Issue number	12
DOIs	https://doi.org/10.1016/S0969-2126(02)00905-X
State	Published - Dec 1 2002

ASJC Scopus subject areas

Structural Biology
Molecular Biology

Keywords

Bacterial GTPase
EngA
Era
KH domain
TM-Der
Tandem G domains

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https://doi.org/10.1016/S0969-2126(02)00905-X

Cite this

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title = "Domain arrangement of Der, a switch protein containing two GTPase domains",

abstract = "The EngA subfamily of essential bacterial GTPases has a unique domain structure consisting of two adjacent GTPase domains (GD1 and GD2) and a C-terminal domain. The structure of Thermotoga maritima Der bound to GDP determined at 1.9 {\AA} resolution reveals a novel domain arrangement in which the GTPase domains pack at either side of the C-terminal domain. Unexpectedly, the C-terminal domain resembles a KH domain, missing the distinctive RNA recognition elements. Conserved motifs of the nucleotide binding site of GD1 are integral parts of the GD1-KH domain interface, suggesting the interactions between these two domains are directly influenced by the GTP/GDP cycling of the protein. In contrast, the GD2-KH domain interface is distal to the GDP binding site of GD2.",

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T1 - Domain arrangement of Der, a switch protein containing two GTPase domains

AU - Robinson, Victoria L.

AU - Hwang, Jihwan

AU - Fox, Eileen

AU - Inouye, Masayori

AU - Stock, Ann M.

PY - 2002/12/1

Y1 - 2002/12/1

N2 - The EngA subfamily of essential bacterial GTPases has a unique domain structure consisting of two adjacent GTPase domains (GD1 and GD2) and a C-terminal domain. The structure of Thermotoga maritima Der bound to GDP determined at 1.9 Å resolution reveals a novel domain arrangement in which the GTPase domains pack at either side of the C-terminal domain. Unexpectedly, the C-terminal domain resembles a KH domain, missing the distinctive RNA recognition elements. Conserved motifs of the nucleotide binding site of GD1 are integral parts of the GD1-KH domain interface, suggesting the interactions between these two domains are directly influenced by the GTP/GDP cycling of the protein. In contrast, the GD2-KH domain interface is distal to the GDP binding site of GD2.

AB - The EngA subfamily of essential bacterial GTPases has a unique domain structure consisting of two adjacent GTPase domains (GD1 and GD2) and a C-terminal domain. The structure of Thermotoga maritima Der bound to GDP determined at 1.9 Å resolution reveals a novel domain arrangement in which the GTPase domains pack at either side of the C-terminal domain. Unexpectedly, the C-terminal domain resembles a KH domain, missing the distinctive RNA recognition elements. Conserved motifs of the nucleotide binding site of GD1 are integral parts of the GD1-KH domain interface, suggesting the interactions between these two domains are directly influenced by the GTP/GDP cycling of the protein. In contrast, the GD2-KH domain interface is distal to the GDP binding site of GD2.

KW - Bacterial GTPase

KW - EngA

KW - Era

KW - KH domain

KW - TM-Der

KW - Tandem G domains

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U2 - https://doi.org/10.1016/S0969-2126(02)00905-X

DO - https://doi.org/10.1016/S0969-2126(02)00905-X

M3 - Article

C2 - 12467572

VL - 10

SP - 1649

EP - 1658

JO - Structure

JF - Structure

SN - 0969-2126

IS - 12

ER -

Domain arrangement of Der, a switch protein containing two GTPase domains

Abstract

ASJC Scopus subject areas

Keywords

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