1MKY

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

Summary for 1MKY

• Entry DOI: 10.2210/pdb1mky/pdb
• Descriptor: Probable GTP-binding protein engA, PHOSPHATE ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: gtpase, enga, der, kh-domain, tandem g-domains, ligand binding protein
• Biological source: Thermotoga maritima
• Total number of polymer chains: 1
• Total formula weight: 51455.17

Authors

Robinson, V.L.,Hwang, J.,Fox, E.,Inouye, M.,Stock, A.M. (deposition date: 2002-08-29, release date: 2003-01-14, Last modification date: 2024-11-20)

Primary citation

Robinson, V.L.,Hwang, J.,Fox, E.,Inouye, M.,Stock, A.M.
Domain Arrangement of Der, a Switch Protein Containing Two GTPase Domains
Structure, 10:1649-1658, 2002

PubMed 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 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.

PubMed: 12467572
DOI: 10.1016/S0969-2126(02)00905-X

Experimental method

X-RAY DIFFRACTION (1.9 Å)