3b9q

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(New page: 200px<br /><applet load="3b9q" size="350" color="white" frame="true" align="right" spinBox="true" caption="3b9q, resolution 1.75&Aring;" /> '''The crystal structur...)
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==Overview==
==Overview==
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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 1.75A 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.
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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.
==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sinning, I.]]
[[Category: Sinning, I.]]
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[[Category: Stengel, K.F.]]
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[[Category: Stengel, K F.]]
[[Category: Wild, K.]]
[[Category: Wild, K.]]
[[Category: MLI]]
[[Category: MLI]]
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[[Category: srp receptor]]
[[Category: srp receptor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:29:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:04:23 2008''

Revision as of 17:04, 21 February 2008


3b9q, resolution 1.75Å

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The crystal structure of cpFtsY from Arabidopsis thaliana

Overview

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.

About this Structure

3B9Q is a Single protein structure of sequence from Arabidopsis thaliana with as ligand. Full crystallographic information is available from OCA.

Reference

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

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