5wfb - Revision history

OCA at 14:15, 13 March 2024

2024-03-13T14:15:40Z

←Older revision		Revision as of 14:15, 13 March 2024
Line 3:		Line 3:
	<StructureSection load='5wfb' size='340' side='right'caption='[[5wfb]], [[Resolution\|resolution]] 1.38Å' scene=''>		<StructureSection load='5wfb' size='340' side='right'caption='[[5wfb]], [[Resolution\|resolution]] 1.38Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5wfb]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WFB OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5WFB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5wfb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WFB FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~TEPSIN~~, ~~C17orf56, ENTHD2 (~~[~~http://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=9606 HUMAN])~~</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]] 1.382Å</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=5wfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wfb OCA], [~~http~~://pdbe.org/5wfb PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5wfb RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5wfb PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5wfb 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=5wfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wfb OCA], [https://pdbe.org/5wfb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wfb RCSB], [https://www.ebi.ac.uk/pdbsum/5wfb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wfb ProSAT]</span></td></tr>
	</table>		</table>
-	~~<div style~~=~~"background-color:#fffaf0;">~~	+	== Function ==
-	=~~= Publication Abstract from PubMed~~ ==	+	[https://www.uniprot.org/uniprot/AP4AT_HUMAN AP4AT_HUMAN]
-	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®/PubMed®, a database of the U~~.S. ~~National Library of Medicine.<br>~~	+
-	</~~div>~~	+
-	~~<div class="pdbe-citations 5wfb" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references~~/>	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Archuleta~~, T L~~]]	+	[[Category: Archuleta TL]]
-	[[Category: Jackson~~, L P]]~~	+	[[Category: Jackson LP]]
-	~~[[Category: Protein trafficking]]~~	+
-	~~[[Category: Protein transport~~]]	+

OCA at 08:10, 27 November 2019

2019-11-27T08:10:44Z

←Older revision		Revision as of 08:10, 27 November 2019
Line 1:		Line 1:

	==Tepsin tENTH domain 1-136.==		==Tepsin tENTH domain 1-136.==
-	<StructureSection load='5wfb' size='340' side='right' caption='[[5wfb]], [[Resolution\|resolution]] 1.38Å' scene=''>	+	<StructureSection load='5wfb' size='340' side='right'caption='[[5wfb]], [[Resolution\|resolution]] 1.38Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5wfb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WFB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WFB FirstGlance]. <br>		<table><tr><td colspan='2'>[[5wfb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WFB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WFB FirstGlance]. <br>
Line 21:		Line 21:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Archuleta, T L]]		[[Category: Archuleta, T L]]
	[[Category: Jackson, L P]]		[[Category: Jackson, L P]]
	[[Category: Protein trafficking]]		[[Category: Protein trafficking]]
	[[Category: Protein transport]]		[[Category: Protein transport]]

OCA at 14:44, 6 November 2017

2017-11-06T14:44:30Z

←Older revision		Revision as of 14:44, 6 November 2017
Line 3:		Line 3:
	<StructureSection load='5wfb' size='340' side='right' caption='[[5wfb]], [[Resolution\|resolution]] 1.38Å' scene=''>		<StructureSection load='5wfb' size='340' side='right' caption='[[5wfb]], [[Resolution\|resolution]] 1.38Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5wfb]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WFB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WFB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5wfb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WFB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WFB 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=5wfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wfb OCA], [http://pdbe.org/5wfb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wfb RCSB], [http://www.ebi.ac.uk/pdbsum/5wfb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wfb ProSAT]</span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TEPSIN, C17orf56, ENTHD2 ([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=5wfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wfb OCA], [http://pdbe.org/5wfb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wfb RCSB], [http://www.ebi.ac.uk/pdbsum/5wfb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wfb ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 19:		Line 20:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Archuleta, T L]]		[[Category: Archuleta, T L]]
	[[Category: Jackson, L P]]		[[Category: Jackson, L P]]
	[[Category: Protein trafficking]]		[[Category: Protein trafficking]]
	[[Category: Protein transport]]		[[Category: Protein transport]]

OCA: Protected "5wfb" [edit=sysop:move=sysop]

2017-08-30T03:57:38Z

Protected "5wfb" [edit=sysop:move=sysop]

←Older revision

Revision as of 03:57, 30 August 2017

OCA: New page: ==Tepsin tENTH domain 1-136.== == Structural highlights ==
2017-08-30T03:57:36Z

New page: ==Tepsin tENTH domain 1-136.== <StructureSection load='5wfb' size='340' side='right' caption='5wfb, resolution 1.38Å' scene=''> == Structural highlights == <table...

New page

==Tepsin tENTH domain 1-136.==
<StructureSection load='5wfb' size='340' side='right' caption='[[5wfb]], [[Resolution|resolution]] 1.38Å' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5wfb]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WFB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WFB 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=5wfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wfb OCA], [http://pdbe.org/5wfb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wfb RCSB], [http://www.ebi.ac.uk/pdbsum/5wfb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wfb ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== 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<ref>PMID:28691777</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5wfb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
TOC
</StructureSection>
[[Category: Archuleta, T L]]
[[Category: Jackson, L P]]
[[Category: Protein trafficking]]
[[Category: Protein transport]]