1mqs

From Proteopedia

(Difference between revisions)

Revision as of 08:54, 21 April 2021

Crystal structure of Sly1p in complex with an N-terminal peptide of Sed5p

Structural highlights

1mqs is a 2 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	1dn1, 1epu, 1fvf, 1fvh
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SLY1_YEAST] Able to suppress the functional loss of YPT1. SLY1 is essential for cell viability. May interact indirectly, or directly with YPT1. [SED5_YEAST] Required for vesicular transport between the endoplasmic reticulum and the Golgi complex. Acts as a target organelle soluble NSF attachment protein receptor (t-SNARE).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bracher A, Weissenhorn W. Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p. EMBO J. 2002 Nov 15;21(22):6114-24. PMID:12426383

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1mqs"

@@ Line 3: / Line 3: @@
 <StructureSection load='1mqs' size='340' side='right'caption='[[1mqs]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mqs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MQS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MQS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mqs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MQS FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dn1|1dn1]], [[1epu|1epu]], [[1fvf|1fvf]], [[1fvh|1fvh]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dn1|1dn1]], [[1epu|1epu]], [[1fvf|1fvf]], [[1fvh|1fvh]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mqs OCA], [http://pdbe.org/1mqs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mqs RCSB], [http://www.ebi.ac.uk/pdbsum/1mqs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mqs ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mqs OCA], [https://pdbe.org/1mqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mqs RCSB], [https://www.ebi.ac.uk/pdbsum/1mqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mqs ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SLY1_YEAST SLY1_YEAST]] Able to suppress the functional loss of YPT1. SLY1 is essential for cell viability. May interact indirectly, or directly with YPT1. [[http://www.uniprot.org/uniprot/SED5_YEAST SED5_YEAST]] Required for vesicular transport between the endoplasmic reticulum and the Golgi complex. Acts as a target organelle soluble NSF attachment protein receptor (t-SNARE).
+[[https://www.uniprot.org/uniprot/SLY1_YEAST SLY1_YEAST]] Able to suppress the functional loss of YPT1. SLY1 is essential for cell viability. May interact indirectly, or directly with YPT1. [[https://www.uniprot.org/uniprot/SED5_YEAST SED5_YEAST]] Required for vesicular transport between the endoplasmic reticulum and the Golgi complex. Acts as a target organelle soluble NSF attachment protein receptor (t-SNARE).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1mqs

From Proteopedia

Revision as of 08:54, 21 April 2021

Crystal structure of Sly1p in complex with an N-terminal peptide of Sed5p

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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