2fh5: Difference between revisions

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[[Image:2fh5.gif|left|200px]]
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{{STRUCTURE_2fh5|  PDB=2fh5  |  SCENE=  }}  
{{STRUCTURE_2fh5|  PDB=2fh5  |  SCENE=  }}  


'''The Structure of the Mammalian SRP Receptor'''
===The Structure of the Mammalian SRP Receptor===




==Overview==
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The eukaryotic signal recognition particle (SRP) and its receptor (SR) play a central role in co-translational targeting of secretory and membrane proteins to the endoplasmic reticulum. The SR is a heterodimeric complex assembled by the two GTPases SRalpha and SRbeta, which is membrane-anchored. Here we present the 2.45-A structure of mammalian SRbeta in its Mg2+ GTP-bound state in complex with the minimal binding domain of SRalpha termed SRX. SRbeta is a member of the Ras-GTPase superfamily closely related to Arf and Sar1, while SRX belongs to the SNARE-like superfamily with a fold also known as longin domain. SRX binds to the P loop and the switch regions of SRbeta-GTP. The binding mode and structural similarity with other GTPase-effector complexes suggests a co-GAP (GTPase-activating protein) function for SRX. Comparison with the homologous yeast structure and other longin domains reveals a conserved adjustable hydrophobic surface within SRX which is of central importance for the SRbeta-GTP:SRX interface. A helix swap in SRX results in the formation of a dimer in the crystal structure. Based on structural conservation we present the SRbeta-GTP:SRX structure as a prototype for conserved interactions in a variety of GTPase regulated targeting events occurring at endomembranes.
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==About this Structure==
==About this Structure==
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[[Category: Signal recognition particle receptor]]
[[Category: Signal recognition particle receptor]]
[[Category: X-ray structure]]
[[Category: X-ray structure]]
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