1z9o
From Proteopedia
(New page: 200px<br /><applet load="1z9o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z9o, resolution 1.90Å" /> '''1.9 Angstrom Crystal...) |
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| - | [[Image:1z9o.gif|left|200px]]<br /><applet load="1z9o" size=" | + | [[Image:1z9o.gif|left|200px]]<br /><applet load="1z9o" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1z9o, resolution 1.90Å" /> | caption="1z9o, resolution 1.90Å" /> | ||
'''1.9 Angstrom Crystal Structure of the Rat VAP-A MSP Homology Domain in Complex with the Rat ORP1 FFAT Motif'''<br /> | '''1.9 Angstrom Crystal Structure of the Rat VAP-A MSP Homology Domain in Complex with the Rat ORP1 FFAT Motif'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The FFAT motif is a targeting signal responsible for localizing a number | + | 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== | ==About this Structure== | ||
| - | 1Z9O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1Z9O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z9O OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
| - | [[Category: Brickner, J | + | [[Category: Brickner, J H.]] |
| - | [[Category: Brunger, A | + | [[Category: Brunger, A T.]] |
| - | [[Category: Fenn, T | + | [[Category: Fenn, T D.]] |
| - | [[Category: Kaiser, S | + | [[Category: Kaiser, S E.]] |
| - | [[Category: Reilein, A | + | [[Category: Reilein, A R.]] |
[[Category: Walter, P.]] | [[Category: Walter, P.]] | ||
[[Category: endoplasmic reticulum]] | [[Category: endoplasmic reticulum]] | ||
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[[Category: vapc]] | [[Category: vapc]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:13:26 2008'' |
Revision as of 14:13, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 16:13:26 2008
Categories: Protein complex | Rattus norvegicus | Brickner, J H. | Brunger, A T. | Fenn, T D. | Kaiser, S E. | Reilein, A R. | Walter, P. | Endoplasmic reticulum | Er | Erg30 | Ffat motif | Immunoglobulin-like beta sheet | Msp homology domain | Orp | Osbp | Oxysterol binding protein | Scs2 | Targeting | Vap-33 | Vap-33a | Vap-a | Vap-b | Vap-c | Vapa | Vapb | Vapc
