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| | <StructureSection load='5wf1' size='340' side='right'caption='[[5wf1]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='5wf1' size='340' side='right'caption='[[5wf1]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5wf1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WF1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WF1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5wf1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WF1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WF1 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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.954Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TEPSIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9796 Equus caballus])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5wf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wf1 OCA], [http://pdbe.org/5wf1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wf1 RCSB], [http://www.ebi.ac.uk/pdbsum/5wf1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wf1 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=5wf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wf1 OCA], [https://pdbe.org/5wf1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wf1 RCSB], [https://www.ebi.ac.uk/pdbsum/5wf1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wf1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/F6SIY5_HORSE F6SIY5_HORSE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Equus caballus]] | | [[Category: Equus caballus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Frazier, M N]] | + | [[Category: Frazier MN]] |
| - | [[Category: Jackson, L P]] | + | [[Category: Jackson LP]] |
| - | [[Category: Monken, A E]] | + | [[Category: Monken AE]] |
| - | [[Category: Protein trafficking]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| Structural highlights
Function
F6SIY5_HORSE
Publication Abstract from PubMed
Tepsin is currently the only accessory trafficking protein identified in adaptor-related protein 4 (AP4) coated vesicles originating at the trans-Golgi network (TGN). The molecular basis for interactions between AP4 subunits and motifs in the tepsin C-terminus have been characterized, but the biological role of tepsin remains unknown. We determined X-ray crystal structures of the tepsin ENTH and VHS/ENTH-like domains. Our data reveal unexpected structural features that suggest key functional differences between these and similar domains in other trafficking proteins. The tepsin ENTH domain lacks helix0, helix8, and a lipid binding pocket found in epsin1/2/3. These results explain why tepsin requires AP4 for its membrane recruitment and further suggest ENTH domains cannot be defined solely as lipid binding modules. The VHS domain lacks helix8 and thus contains fewer helices than other VHS domains. Structural data explain biochemical and biophysical evidence that tepsin VHS does not mediate known VHS functions, including recognition of dileucine-based cargo motifs or ubiquitin. Structural comparisons indicate the domains are very similar to each other, and phylogenetic analysis reveals their evolutionary pattern within the domain superfamily. Phylogenetics and comparative genomics further show tepsin within a monophyletic clade that diverged away from epsins early in evolutionary history (~1,500 million years ago). Together, these data provide the first detailed molecular view of tepsin and suggest tepsin structure and function diverged away from other epsins. More broadly, these data highlight the challenges inherent in classifying and understanding protein function based only on sequence and structure.
Structure and evolution of ENTH and VHS/ENTH-like domains in tepsin.,Archuleta TL, Frazier MN, Monken AE, Kendall AK, Harp J, McCoy AJ, Creanza N, Jackson LP Traffic. 2017 Jul 10. doi: 10.1111/tra.12499. PMID:28691777[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Archuleta TL, Frazier MN, Monken AE, Kendall AK, Harp J, McCoy AJ, Creanza N, Jackson LP. Structure and evolution of ENTH and VHS/ENTH-like domains in tepsin. Traffic. 2017 Jul 10. doi: 10.1111/tra.12499. PMID:28691777 doi:http://dx.doi.org/10.1111/tra.12499
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