4hrs - Revision history

OCA at 11:44, 1 March 2024

OCA — Fri, 01 Mar 2024 11:44:17 GMT

←Older revision		Revision as of 11:44, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4hrs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haloferax_volcanii_DS2 Haloferax volcanii DS2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HRS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HRS FirstGlance]. <br>		<table><tr><td colspan='2'>[[4hrs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haloferax_volcanii_DS2 Haloferax volcanii DS2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HRS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HRS FirstGlance]. <br>
-	</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=4hrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hrs OCA], [https://pdbe.org/4hrs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hrs RCSB], [https://www.ebi.ac.uk/pdbsum/4hrs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hrs 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]] 2.3Å</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=4hrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hrs OCA], [https://pdbe.org/4hrs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hrs RCSB], [https://www.ebi.ac.uk/pdbsum/4hrs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hrs ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/SAMP2_HALVD SAMP2_HALVD] Protein modifier that is covalently attached to lysine residues of substrate proteins. The tagging system is termed SAMPylation. It is not known whether it is implicated in the targeting of proteins to the proteasome for degradation. Is able to form polymeric chains with itself at Lys-58, similar to ubiquitin and other ubiquitin-like proteins.		[https://www.uniprot.org/uniprot/SAMP2_HALVD SAMP2_HALVD] Protein modifier that is covalently attached to lysine residues of substrate proteins. The tagging system is termed SAMPylation. It is not known whether it is implicated in the targeting of proteins to the proteasome for degradation. Is able to form polymeric chains with itself at Lys-58, similar to ubiquitin and other ubiquitin-like proteins.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The discovery of ubiquitin-like small archaeal modifier protein 2 (SAMP2) that forms covalent polymeric chains in Haloferax volcanii has generated tremendous interest in the function and regulation of this protein. At present, it remains unclear whether the Hfx. volcanii modifier protein SAMP1 has such polyubiquitinating-like activity. Although SAMP1 and SAMP2 use the same conjugation machinery to modify their target proteins, each can impart distinct functional consequences. To better understand the mechanism of SAMP2 conjugation, we have sought to characterize the biophysical and structural properties of the protein from Hfx. volcanii. SAMP2 is only partially structured under mesohalic solution conditions and adopts a well-folded compact conformation in the presence of 2.5M of NaCl. Its 2.3-A-resolution crystal structure reveals a characteristic alpha/beta central core domain and a unique beta-hinge motif. This motif anchors an unusual C-terminal extension comprising the diglycine tail as well as two lysine residues that can potentially serve to interlink SAMP2 moieties. Mutational alternation of the structural malleability of this beta-hinge motif essentially abolishes the conjugation activity of SAMP2 in vivo. In addition, NMR structural studies of the putative ubiquitin-like protein HVO_2177 from Hfx. volcanii show that like SAMP1, HVO_2177 forms a classic beta-grasp fold in a salt-independent manner. These results provide insights into the structure-function relationship of sampylating proteins of fundamental importance in post-translational protein modification and environmental cues in Archaea.
-
-	Crystal structure of the ubiquitin-like small archaeal modifier protein 2 from Haloferax volcanii.,Li Y, Maciejewski MW, Martin J, Jin K, Zhang Y, Maupin-Furlow JA, Hao B Protein Sci. 2013 Jul 2. doi: 10.1002/pro.2305. PMID:23821306<ref>PMID:23821306</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4hrs" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:08, 9 November 2022

OCA — Wed, 09 Nov 2022 08:08:54 GMT

←Older revision		Revision as of 08:08, 9 November 2022
Line 1:		Line 1:

	==Crystal structure of H. volcanii small archaeal modifier protein 2==		==Crystal structure of H. volcanii small archaeal modifier protein 2==
-	<StructureSection load='4hrs' size='340' side='right' caption='[[4hrs]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='4hrs' size='340' side='right'caption='[[4hrs]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4hrs]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Halvd Halvd~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HRS OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4HRS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4hrs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haloferax_volcanii_DS2 Haloferax volcanii DS2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HRS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HRS FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4hro\|4hro]]</td></tr>~~	+	</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=4hrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hrs OCA], [https://pdbe.org/4hrs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hrs RCSB], [https://www.ebi.ac.uk/pdbsum/4hrs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hrs ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HVO_0202 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=309800 HALVD])</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=4hrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hrs OCA], [~~http~~://pdbe.org/4hrs PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4hrs RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4hrs PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4hrs ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/SAMP2_HALVD SAMP2_HALVD]] Protein modifier that is covalently attached to lysine residues of substrate proteins. The tagging system is termed SAMPylation. It is not known whether it is implicated in the targeting of proteins to the proteasome for degradation. Is able to form polymeric chains with itself at Lys-58, similar to ubiquitin and other ubiquitin-like proteins.	+	[https://www.uniprot.org/uniprot/SAMP2_HALVD SAMP2_HALVD] Protein modifier that is covalently attached to lysine residues of substrate proteins. The tagging system is termed SAMPylation. It is not known whether it is implicated in the targeting of proteins to the proteasome for degradation. Is able to form polymeric chains with itself at Lys-58, similar to ubiquitin and other ubiquitin-like proteins.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Halvd~~]]	+	[[Category: Haloferax volcanii DS2]]
-	[[Category: ~~Hao, B~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Beta-grasp fold]]~~	+	[[Category: Hao B]]
-	~~[[Category: Beta-hinge motif]]~~	+
-	~~[[Category: Protein binding]]~~	+
-	~~[[Category: Small ubiquitin-like modifier~~]]	+

OCA at 13:54, 5 August 2016

OCA — Fri, 05 Aug 2016 13:54:37 GMT

←Older revision		Revision as of 13:54, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of H. volcanii small archaeal modifier protein 2==		==Crystal structure of H. volcanii small archaeal modifier protein 2==
	<StructureSection load='4hrs' size='340' side='right' caption='[[4hrs]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='4hrs' size='340' side='right' caption='[[4hrs]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4hrs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Haloferax_volcanii_ds2 Haloferax volcanii ds2~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HRS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HRS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4hrs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Halvd Halvd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HRS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HRS FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4hro\|4hro]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4hro\|4hro]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HVO_0202 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=309800 ~~Haloferax volcanii DS2~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HVO_0202 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=309800 HALVD])</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=4hrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hrs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hrs RCSB], [http://www.ebi.ac.uk/pdbsum/4hrs 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=4hrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hrs OCA], [http://pdbe.org/4hrs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hrs RCSB], [http://www.ebi.ac.uk/pdbsum/4hrs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hrs ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4hrs" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Haloferax volcanii ds2~~]]	+	[[Category: Halvd]]
	[[Category: Hao, B]]		[[Category: Hao, B]]
	[[Category: Beta-grasp fold]]		[[Category: Beta-grasp fold]]

OCA at 03:02, 25 December 2014

OCA — Thu, 25 Dec 2014 03:02:40 GMT

←Older revision		Revision as of 03:02, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4hrs\| PDB=4hrs \| SCENE= }}~~	+	==Crystal structure of H. volcanii small archaeal modifier protein 2==
-	===Crystal structure of H. volcanii small archaeal modifier protein 2===	+	<StructureSection load='4hrs' size='340' side='right' caption='[[4hrs]], [[Resolution\|resolution]] 2.30Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23821306}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4hrs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Haloferax_volcanii_ds2 Haloferax volcanii ds2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HRS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HRS FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4hro\|4hro]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HVO_0202 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=309800 Haloferax volcanii DS2])</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=4hrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hrs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hrs RCSB], [http://www.ebi.ac.uk/pdbsum/4hrs PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/SAMP2_HALVD SAMP2_HALVD]] Protein modifier that is covalently attached to lysine residues of substrate proteins. The tagging system is termed SAMPylation. It is not known whether it is implicated in the targeting of proteins to the proteasome for degradation. Is able to form polymeric chains with itself at Lys-58, similar to ubiquitin and other ubiquitin-like proteins.		[[http://www.uniprot.org/uniprot/SAMP2_HALVD SAMP2_HALVD]] Protein modifier that is covalently attached to lysine residues of substrate proteins. The tagging system is termed SAMPylation. It is not known whether it is implicated in the targeting of proteins to the proteasome for degradation. Is able to form polymeric chains with itself at Lys-58, similar to ubiquitin and other ubiquitin-like proteins.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The discovery of ubiquitin-like small archaeal modifier protein 2 (SAMP2) that forms covalent polymeric chains in Haloferax volcanii has generated tremendous interest in the function and regulation of this protein. At present, it remains unclear whether the Hfx. volcanii modifier protein SAMP1 has such polyubiquitinating-like activity. Although SAMP1 and SAMP2 use the same conjugation machinery to modify their target proteins, each can impart distinct functional consequences. To better understand the mechanism of SAMP2 conjugation, we have sought to characterize the biophysical and structural properties of the protein from Hfx. volcanii. SAMP2 is only partially structured under mesohalic solution conditions and adopts a well-folded compact conformation in the presence of 2.5M of NaCl. Its 2.3-A-resolution crystal structure reveals a characteristic alpha/beta central core domain and a unique beta-hinge motif. This motif anchors an unusual C-terminal extension comprising the diglycine tail as well as two lysine residues that can potentially serve to interlink SAMP2 moieties. Mutational alternation of the structural malleability of this beta-hinge motif essentially abolishes the conjugation activity of SAMP2 in vivo. In addition, NMR structural studies of the putative ubiquitin-like protein HVO_2177 from Hfx. volcanii show that like SAMP1, HVO_2177 forms a classic beta-grasp fold in a salt-independent manner. These results provide insights into the structure-function relationship of sampylating proteins of fundamental importance in post-translational protein modification and environmental cues in Archaea.

-	~~==About this Structure==~~	+	Crystal structure of the ubiquitin-like small archaeal modifier protein 2 from Haloferax volcanii.,Li Y, Maciejewski MW, Martin J, Jin K, Zhang Y, Maupin-Furlow JA, Hao B Protein Sci. 2013 Jul 2. doi: 10.1002/pro.2305. PMID:23821306<ref>PMID:23821306</ref>
-	~~[[4hrs]] is a 1 chain~~ structure ~~with sequence~~ from ~~[http://en.wikipedia.org/wiki/Haloferax_volcanii_ds2~~ Haloferax volcanii ~~ds2]~~. ~~Full crystallographic information is available from [http~~:/~~/oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4HRS OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:023821306</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Haloferax volcanii ds2]]		[[Category: Haloferax volcanii ds2]]
-	[[Category: Hao, B.]]	+	[[Category: Hao, B]]
	[[Category: Beta-grasp fold]]		[[Category: Beta-grasp fold]]
	[[Category: Beta-hinge motif]]		[[Category: Beta-hinge motif]]
	[[Category: Protein binding]]		[[Category: Protein binding]]
	[[Category: Small ubiquitin-like modifier]]		[[Category: Small ubiquitin-like modifier]]

OCA at 20:56, 7 August 2013

OCA — Wed, 07 Aug 2013 20:56:34 GMT

←Older revision		Revision as of 20:56, 7 August 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4hrs\| PDB=4hrs \| SCENE= }}
		+	===Crystal structure of H. volcanii small archaeal modifier protein 2===
		+	{{ABSTRACT_PUBMED_23821306}}

-	The ~~entry 4hrs~~ is ~~ON HOLD until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/SAMP2_HALVD SAMP2_HALVD]] Protein modifier that is covalently attached to lysine residues of substrate proteins. The tagging system is termed SAMPylation. It is not known whether it is implicated in the targeting of proteins to the proteasome for degradation. Is able to form polymeric chains with itself at Lys-58, similar to ubiquitin and other ubiquitin-like proteins.

-	~~Authors~~: ~~Hao, B~~.	+	==About this Structure==
		+	[[4hrs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Haloferax_volcanii_ds2 Haloferax volcanii ds2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HRS OCA].

-	~~Description~~: ~~Crystal structure of H.~~ volcanii ~~small archaeal~~ modifier ~~protein 2~~	+	==Reference==
		+	<ref group="xtra">PMID:023821306</ref><references group="xtra"/><references/>
		+	[[Category: Haloferax volcanii ds2]]
		+	[[Category: Hao, B.]]
		+	[[Category: Beta-grasp fold]]
		+	[[Category: Beta-hinge motif]]
		+	[[Category: Protein binding]]
		+	[[Category: Small ubiquitin-like modifier]]

OCA: Protected "4hrs" [edit=sysop:move=sysop]

OCA — Thu, 08 Nov 2012 13:25:42 GMT

Protected "4hrs" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:25, 8 November 2012

OCA: New page: '''Unreleased structure''' The entry 4hrs is ON HOLD until Paper Publication Authors: Hao, B. Description: Crystal structure of H. volcanii small archaeal modifier protein 2

OCA — Thu, 08 Nov 2012 13:25:41 GMT

New page: '''Unreleased structure''' The entry 4hrs is ON HOLD until Paper Publication Authors: Hao, B. Description: Crystal structure of H. volcanii small archaeal modifier protein 2

New page

'''Unreleased structure'''

The entry 4hrs is ON HOLD until Paper Publication

Authors: Hao, B.

Description: Crystal structure of H. volcanii small archaeal modifier protein 2