5wf2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: ==Tepsin VHS/ENTH-like Native== <StructureSection load='5wf2' size='340' side='right' caption='5wf2, resolution 1.85&Aring;' scene=''> == Structural highlights == <tabl...)
Current revision (14:15, 13 March 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
==Tepsin VHS/ENTH-like Native==
==Tepsin VHS/ENTH-like Native==
-
<StructureSection load='5wf2' size='340' side='right' caption='[[5wf2]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
+
<StructureSection load='5wf2' size='340' side='right'caption='[[5wf2]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5wf2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WF2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WF2 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5wf2]] 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=5WF2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WF2 FirstGlance]. <br>
-
</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=5wf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wf2 OCA], [http://pdbe.org/5wf2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wf2 RCSB], [http://www.ebi.ac.uk/pdbsum/5wf2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wf2 ProSAT]</span></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]] 1.851&#8491;</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=5wf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wf2 OCA], [https://pdbe.org/5wf2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wf2 RCSB], [https://www.ebi.ac.uk/pdbsum/5wf2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wf2 ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/F6SIY5_HORSE F6SIY5_HORSE]
-
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<ref>PMID:28691777</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 5wf2" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Frazier, M N]]
+
[[Category: Equus caballus]]
-
[[Category: Jackson, L P]]
+
[[Category: Large Structures]]
-
[[Category: Monken, A E]]
+
[[Category: Frazier MN]]
-
[[Category: Protein trafficking]]
+
[[Category: Jackson LP]]
-
[[Category: Protein transport]]
+
[[Category: Monken AE]]

Current revision

Tepsin VHS/ENTH-like Native

PDB ID 5wf2

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5wf2"
Personal tools