1mky

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Revision as of 19:22, 20 November 2007

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spinqualitylabelsall models 1mky, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structural Analysis of the Domain Interactions in Der, a Switch Protein Containing Two GTPase Domains

Overview

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 A 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.

About this Structure

1MKY is a Single protein structure of sequence from Thermotoga maritima with PO4 and GDP as ligands. Full crystallographic information is available from OCA.

Reference

Domain arrangement of Der, a switch protein containing two GTPase domains., Robinson VL, Hwang J, Fox E, Inouye M, Stock AM, Structure. 2002 Dec;10(12):1649-58. PMID:12467572

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