The crystal structure of cpFtsY from Arabidopsis thalianaThe crystal structure of cpFtsY from Arabidopsis thaliana

Structural highlights

3b9q is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
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Evolutionary Conservation

 

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Publication Abstract from PubMed

Two GTPases in the signal recognition particle and its receptor (FtsY) regulate protein targeting to the membrane by formation of a heterodimeric complex. The activation of both GTPases in the complex is essential for protein translocation. We present the crystal structure of chloroplast FtsY (cpFtsY) at 1.75 A resolution. The comparison with FtsY structures in different nucleotide bound states shows structural changes relevant for GTPase activation and provides insights in how cpFtsY is pre-organized for complex formation with cpSRP54. The structure contains an amino-terminal amphipathic helix similar to the membrane targeting sequence of Escherichia coli FtsY. In cpFtsY this motif is extended, which might be responsible for the enhanced attachment of the protein to the thylakoid membrane.

The structure of the chloroplast signal recognition particle (SRP) receptor reveals mechanistic details of SRP GTPase activation and a conserved membrane targeting site.,Stengel KF, Holdermann I, Wild K, Sinning I FEBS Lett. 2007 Dec 11;581(29):5671-6. Epub 2007 Nov 20. PMID:18022392[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Stengel KF, Holdermann I, Wild K, Sinning I. The structure of the chloroplast signal recognition particle (SRP) receptor reveals mechanistic details of SRP GTPase activation and a conserved membrane targeting site. FEBS Lett. 2007 Dec 11;581(29):5671-6. Epub 2007 Nov 20. PMID:18022392 doi:10.1016/j.febslet.2007.11.024

3b9q, resolution 1.75Å

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