1mqs
From Proteopedia
(New page: 200px<br /><applet load="1mqs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mqs, resolution 3.00Å" /> '''Crystal structure of...) |
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| - | [[Image:1mqs.jpg|left|200px]]<br /><applet load="1mqs" size=" | + | [[Image:1mqs.jpg|left|200px]]<br /><applet load="1mqs" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mqs, resolution 3.00Å" /> | caption="1mqs, resolution 3.00Å" /> | ||
'''Crystal structure of Sly1p in complex with an N-terminal peptide of Sed5p'''<br /> | '''Crystal structure of Sly1p in complex with an N-terminal peptide of Sed5p'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cytosolic Sec1/munc18-like proteins (SM proteins) are recruited to | + | Cytosolic Sec1/munc18-like proteins (SM proteins) are recruited to membrane fusion sites by interaction with syntaxin-type SNARE proteins, constituting indispensable positive regulators of intracellular membrane fusion. Here we present the crystal structure of the yeast SM protein Sly1p in complex with a short N-terminal peptide derived from the Golgi-resident syntaxin Sed5p. Sly1p folds, similarly to neuronal Sec1, into a three-domain arch-shaped assembly, and Sed5p interacts in a helical conformation predominantly with domain I of Sly1p on the opposite site of the nSec1/syntaxin-1-binding site. Sequence conservation of the major interactions suggests that homologues of Sly1p as well as the paralogous Vps45p group bind their respective syntaxins in the same way. Furthermore, we present indirect evidence that nSec1 might be able to contact syntaxin 1 in a similar fashion. The observed Sly1p-Sed5p interaction mode therefore indicates how SM proteins can stay associated with the assembling fusion machinery in order to participate in late fusion steps. |
==About this Structure== | ==About this Structure== | ||
| - | 1MQS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http:// | + | 1MQS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MQS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: syntaxin]] | [[Category: syntaxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:07 2008'' |
Revision as of 11:58, 21 February 2008
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Crystal structure of Sly1p in complex with an N-terminal peptide of Sed5p
Overview
Cytosolic Sec1/munc18-like proteins (SM proteins) are recruited to membrane fusion sites by interaction with syntaxin-type SNARE proteins, constituting indispensable positive regulators of intracellular membrane fusion. Here we present the crystal structure of the yeast SM protein Sly1p in complex with a short N-terminal peptide derived from the Golgi-resident syntaxin Sed5p. Sly1p folds, similarly to neuronal Sec1, into a three-domain arch-shaped assembly, and Sed5p interacts in a helical conformation predominantly with domain I of Sly1p on the opposite site of the nSec1/syntaxin-1-binding site. Sequence conservation of the major interactions suggests that homologues of Sly1p as well as the paralogous Vps45p group bind their respective syntaxins in the same way. Furthermore, we present indirect evidence that nSec1 might be able to contact syntaxin 1 in a similar fashion. The observed Sly1p-Sed5p interaction mode therefore indicates how SM proteins can stay associated with the assembling fusion machinery in order to participate in late fusion steps.
About this Structure
1MQS is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p., Bracher A, Weissenhorn W, EMBO J. 2002 Nov 15;21(22):6114-24. PMID:12426383
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