Domain arrangement of Der, a switch protein containing two GTPase domains.
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.
Robinson
Victoria L
VL
Howard Hughes Medical Institute and Center for Advanced Biotechnology and Medicine, 679 Hoes Lane, Piscataway, NJ 08854, USA.
Hwang
Jihwan
J
Fox
Eileen
E
Inouye
Masayori
M
Stock
Ann M
AM
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D018360:Crystallography, X-Ray; D020558:GTP Phosphohydrolases / Q000737:chemistry*; D006160:Guanosine Triphosphate / Q000378:metabolism; D006868:Hydrolysis; D008958:Models, Molecular; D016296:Mutagenesis; D011487:Protein Conformation; D020124:Thermotoga maritima / Q000201:enzymology*
D001426:Bacterial Proteins; D006160:Guanosine Triphosphate; D020558:GTP Phosphohydrolases