期刊
FEBS LETTERS
卷 581, 期 29, 页码 5671-5676出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2007.11.024
关键词
chloroplast SRP system; protein targeting; cpFtsY; SRP GTPase; membrane targeting sequence
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 angstrom 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. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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