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1yx6

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Revision as of 16:19, 11 September 2015

Solution Structure of S5a UIM-2/Ubiquitin Complex

Structural highlights

1yx6 is a 2 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1d3z, 1tbe, 1yx4, 1yx5
Gene:	PSMD4, MCB1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[PSD4_HUMAN] Guanine nucleotide exchange factor for ARF6 and ARL14/ARF7. Through ARL14 activation, controls the movement of MHC class II-containing vesicles along the actin cytoskeleton in dendritic cells. Involved in membrane recycling. Interacts with several phosphatidylinositol phosphate species, including phosphatidylinositol 3,4-bisphosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 4,5-bisphosphate.^[1] ^[2]

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

Ubiquitin is a key regulatory molecule in diverse cellular events. How cells determine the outcome of ubiquitylation remains unclear; however, a likely determinant is the specificity of ubiquitin receptor proteins for polyubiquitin chains of certain length and linkage. Proteasome subunit S5a contains two ubiquitin-interacting motifs (UIMs) through which it recruits ubiquitylated substrates to the proteasome for their degradation. Here, we report the structure of S5a (196-306) alone and complexed with two monoubiquitin molecules. This construct contains the two UIMs of S5a and we reveal their different ubiquitin-binding mechanisms and provide a rationale for their unique specificities for different ubiquitin-like domains. Furthermore, we provide direct evidence that S5a (196-306) binds either K63-linked or K48-linked polyubiquitin, and in both cases prefers longer chains. On the basis of these results we present a model for how S5a and other ubiquitin-binding proteins recognize polyubiquitin.

Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition.,Wang Q, Young P, Walters KJ J Mol Biol. 2005 May 6;348(3):727-39. PMID:15826667^[3]

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

References

↑ Derrien V, Couillault C, Franco M, Martineau S, Montcourrier P, Houlgatte R, Chavrier P. A conserved C-terminal domain of EFA6-family ARF6-guanine nucleotide exchange factors induces lengthening of microvilli-like membrane protrusions. J Cell Sci. 2002 Jul 15;115(Pt 14):2867-79. PMID:12082148
↑ Paul P, van den Hoorn T, Jongsma ML, Bakker MJ, Hengeveld R, Janssen L, Cresswell P, Egan DA, van Ham M, Ten Brinke A, Ovaa H, Beijersbergen RL, Kuijl C, Neefjes J. A Genome-wide multidimensional RNAi screen reveals pathways controlling MHC class II antigen presentation. Cell. 2011 Apr 15;145(2):268-83. doi: 10.1016/j.cell.2011.03.023. Epub 2011 Mar, 31. PMID:21458045 doi:http://dx.doi.org/10.1016/j.cell.2011.03.023
↑ Wang Q, Young P, Walters KJ. Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition. J Mol Biol. 2005 May 6;348(3):727-39. PMID:15826667 doi:http://dx.doi.org/10.1016/j.jmb.2005.03.007

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1yx6"

@@ Line 2: / Line 2: @@
 <StructureSection load='1yx6' size='340' side='right' caption='[[1yx6]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1yx6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YX6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YX6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1yx6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YX6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YX6 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d3z|1d3z]], [[1tbe|1tbe]], [[1yx4|1yx4]], [[1yx5|1yx5]]</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PSMD4, MCB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PSMD4, MCB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1yx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yx6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yx6 RCSB], [http://www.ebi.ac.uk/pdbsum/1yx6 PDBsum]</span></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=1yx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yx6 OCA], [http://pdbe.org/1yx6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yx6 RCSB], [http://www.ebi.ac.uk/pdbsum/1yx6 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/PSD4_HUMAN PSD4_HUMAN]] Guanine nucleotide exchange factor for ARF6 and ARL14/ARF7. Through ARL14 activation, controls the movement of MHC class II-containing vesicles along the actin cytoskeleton in dendritic cells. Involved in membrane recycling. Interacts with several phosphatidylinositol phosphate species, including phosphatidylinositol 3,4-bisphosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 4,5-bisphosphate.<ref>PMID:12082148</ref> <ref>PMID:21458045</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 25: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1yx6" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 33: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Homo sapiens]]
+[[Category: Human]]
 [[Category: Walters, K J]]
 [[Category: Wang, Q]]

1yx6

From Proteopedia

Revision as of 16:19, 11 September 2015

Solution Structure of S5a UIM-2/Ubiquitin Complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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