Novel Protein and Mg2+ Configurations in the Mg2+GDP Complex of the SRP GTPase Ffh

Pamela J. Focia, Hena Alam, Thanh Lu, Ursula D. Ramirez, Douglas M. Freymann*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


Ffh is the signal sequence recognition and targeting subunit of the prokaryotic signal recognition particle (SRP). Previous structural studies of the NG GTPase domain of Ffh demonstrated magnesium-dependent and magnesium-independent binding conformations for GDP and GMPPNP that are believed to reflect novel mechanisms for exchange and activation in this member of the GTPase superfamily. The current study of the NG GTPase bound to Mg 2+GDP reveals two new binding conformations-in the first the magnesium interactions are similar to those seen previously, however, the protein undergoes a conformational change that brings a conserved aspartate into its second coordination sphere. In the second, the protein conformation is similar to that seen previously, but the magnesium coordination sphere is disrupted so that only five oxygen ligands are present. The loss of the coordinating water molecule, at the position that would be occupied by the oxygen of the γ-phosphate of GTP, is consistent with that position being privileged for exchange during phosphate release. The available structures of the GDP-bound protein provide a series of structural snapshots that illuminate steps along the pathway of GDP release following GTP hydrolysis.

Original languageEnglish (US)
Pages (from-to)222-230
Number of pages9
JournalProteins: Structure, Function and Genetics
Issue number2
StatePublished - Feb 1 2004


  • Crystallography
  • Ffh
  • FtsY
  • GTPase
  • Magnesium coordination
  • SRP54
  • Signal recognition particle (SRP)

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology
  • Biochemistry


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