1mky | pdb_00001mky
Structural Analysis of the Domain Interactions in Der, a Switch Protein Containing Two GTPase Domains
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| 1mky, resolution 1.90Å | |||||||||||||
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| Ligands: | GDP, MSE, PO4 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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