Domain arrangement of Der, a switch protein containing two GTPase domains

Victoria L. Robinson, Jihwan Hwang, Eileen Fox, Masayori Inouye, Ann M. Stock

Research output: Contribution to journalArticlepeer-review

57 Scopus citations

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 Å 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.

Original languageEnglish (US)
Pages (from-to)1649-1658
Number of pages10
JournalStructure
Volume10
Issue number12
DOIs
StatePublished - Dec 1 2002

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Keywords

  • Bacterial GTPase
  • EngA
  • Era
  • KH domain
  • TM-Der
  • Tandem G domains

Fingerprint

Dive into the research topics of 'Domain arrangement of Der, a switch protein containing two GTPase domains'. Together they form a unique fingerprint.

Cite this