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| | <StructureSection load='2a6x' size='340' side='right'caption='[[2a6x]], [[Resolution|resolution]] 1.55Å' scene=''> | | <StructureSection load='2a6x' size='340' side='right'caption='[[2a6x]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2a6x]] 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=2A6X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A6X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2a6x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A6X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A6X FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1gv9|1gv9]], [[1r1z|1r1z]], [[2a6v|2a6v]], [[2a6w|2a6w]], [[2a6y|2a6y]], [[2a6z|2a6z]], [[2a70|2a70]], [[2a71|2a71]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></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=2a6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a6x OCA], [https://pdbe.org/2a6x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a6x RCSB], [https://www.ebi.ac.uk/pdbsum/2a6x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a6x 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=2a6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a6x OCA], [https://pdbe.org/2a6x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a6x RCSB], [https://www.ebi.ac.uk/pdbsum/2a6x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a6x ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/EMP46_YEAST EMP46_YEAST] Involved in the secretion of glycoproteins and in nucleus architecture and gene silencing.<ref>PMID:12134087</ref> <ref>PMID:12206772</ref> <ref>PMID:14627716</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kanoh, A]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Kato, R]] | + | [[Category: Kanoh A]] |
| - | [[Category: Nakano, A]] | + | [[Category: Kato R]] |
| - | [[Category: Structural genomic]] | + | [[Category: Nakano A]] |
| - | [[Category: Sato, K]] | + | [[Category: Sato K]] |
| - | [[Category: Satoh, T]] | + | [[Category: Satoh T]] |
| - | [[Category: Wakatsuki, S]] | + | [[Category: Wakatsuki S]] |
| - | [[Category: Yamashita, K]] | + | [[Category: Yamashita K]] |
| - | [[Category: Beta sandwich]]
| + | |
| - | [[Category: Carbohydrate binding protein]]
| + | |
| - | [[Category: Cargo receptor]]
| + | |
| - | [[Category: National project on protein structural and functional analyse]]
| + | |
| - | [[Category: Nppsfa]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
Function
EMP46_YEAST Involved in the secretion of glycoproteins and in nucleus architecture and gene silencing.[1] [2] [3]
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
Emp46p and Emp47p are type I membrane proteins, which cycle between the endoplasmic reticulum (ER) and the Golgi apparatus by vesicles coated with coat protein complexes I and II (COPI and COPII). They are considered to function as cargo receptors for exporting N-linked glycoproteins from the ER. We have determined crystal structures of the carbohydrate recognition domains (CRDs) of Emp46p and Emp47p of Saccharomyces cerevisiae, in the absence and presence of metal ions. Both proteins fold as a beta-sandwich, and resemble that of the mammalian ortholog, p58/ERGIC-53. However, the nature of metal binding is distinct from that of Ca(2+)-dependent p58/ERGIC-53. Interestingly, the CRD of Emp46p does not bind Ca(2+) ion but instead binds K(+) ion at the edge of a concave beta-sheet whose position is distinct from the corresponding site of the Ca(2+) ion in p58/ERGIC-53. Binding of K(+) ion to Emp46p appears essential for transport of a subset of glycoproteins because the Y131F mutant of Emp46p, which cannot bind K(+) ion fails to rescue the transport in disruptants of EMP46 and EMP47 genes. In contrast the CRD of Emp47p binds no metal ions at all. Furthermore, the CRD of Emp46p binds to glycoproteins carrying high mannosetype glycans and the is promoted by binding not the addition of Ca(2+) or K(+) ion in These results suggest that Emp46p can be regarded as a Ca(2+)-independent intracellular lectin at the ER exit sites.
Structures of the carbohydrate recognition domain of Ca2+-independent cargo receptors Emp46p and Emp47p.,Satoh T, Sato K, Kanoh A, Yamashita K, Yamada Y, Igarashi N, Kato R, Nakano A, Wakatsuki S J Biol Chem. 2006 Apr 14;281(15):10410-9. Epub 2006 Jan 26. PMID:16439369[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sato K, Nakano A. Emp47p and its close homolog Emp46p have a tyrosine-containing endoplasmic reticulum exit signal and function in glycoprotein secretion in Saccharomyces cerevisiae. Mol Biol Cell. 2002 Jul;13(7):2518-32. PMID:12134087 doi:10.1091/mbc.e02-01-0027
- ↑ Teixeira MT, Dujon B, Fabre E. Genome-wide nuclear morphology screen identifies novel genes involved in nuclear architecture and gene-silencing in Saccharomyces cerevisiae. J Mol Biol. 2002 Aug 23;321(4):551-61. PMID:12206772
- ↑ Sato K, Nakano A. Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting. J Biol Chem. 2004 Jan 9;279(2):1330-5. Epub 2003 Nov 19. PMID:14627716 doi:10.1074/jbc.C300457200
- ↑ Satoh T, Sato K, Kanoh A, Yamashita K, Yamada Y, Igarashi N, Kato R, Nakano A, Wakatsuki S. Structures of the carbohydrate recognition domain of Ca2+-independent cargo receptors Emp46p and Emp47p. J Biol Chem. 2006 Apr 14;281(15):10410-9. Epub 2006 Jan 26. PMID:16439369 doi:10.1074/jbc.M512258200
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