1z9o

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spinqualitylabelsall models 1z9o, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

1.9 Angstrom Crystal Structure of the Rat VAP-A MSP Homology Domain in Complex with the Rat ORP1 FFAT Motif

Overview

The FFAT motif is a targeting signal responsible for localizing a number, of proteins to the cytosolic surface of the endoplasmic reticulum (ER) and, to the nuclear membrane. FFAT motifs bind to members of the highly, conserved VAP protein family, which are tethered to the cytoplasmic face, of the ER by a C-terminal transmembrane domain. We have solved crystal, structures of the rat VAP-A MSP homology domain alone and in complex with, an FFAT motif. The co-crystal structure was used to design a VAP mutant, that disrupts rat and yeast VAP-FFAT interactions in vitro. The FFAT, binding-defective mutant also blocked function of the VAP homolog Scs2p in, yeast. Finally, overexpression of the FFAT binding-defective VAP in COS7, cells dramatically altered ER morphology. Our data establish the, structural basis of FFAT-mediated ER targeting and suggest that, FFAT-targeted proteins play an important role in determining ER, morphology.

About this Structure

1Z9O is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Structural basis of FFAT motif-mediated ER targeting., Kaiser SE, Brickner JH, Reilein AR, Fenn TD, Walter P, Brunger AT, Structure. 2005 Jul;13(7):1035-45. PMID:16004875

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