Structural highlights
Function
[DER_THEMA] GTPase that plays an essential role in the late steps of ribosome biogenesis (By similarity). Has GTPase activity but no ATPase activity. GTP, GDP, and dGTP but not GMP, ATP, CTP, and UTP compete for GTP binding.[HAMAP-Rule:MF_00195]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Robinson VL, Hwang J, Fox E, Inouye M, Stock AM. Domain arrangement of Der, a switch protein containing two GTPase domains. Structure. 2002 Dec;10(12):1649-58. PMID:12467572