3b9q
The crystal structure of cpFtsY from Arabidopsis thalianaThe crystal structure of cpFtsY from Arabidopsis thaliana
Structural highlights
FunctionCFTSY_ARATH Signal recognition particle receptor protein. Binds GTP specifically. The GTPase activity is inhibited by the N-terminus of the protein until binding to the thylakoid membrane. Activates the GTPase activity of FFC/cpSRP54 when bound to the cpSRP complex. Required for light-harvesting chlorophyll a/b-binding protein (LHCP) integration into thylakoids. Might be also functionally linked to the Sec translocation machinery.[1] [2] [3] [4] [5] [6] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTwo 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[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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