5xqm - Revision history

OCA at 07:28, 1 May 2024

OCA — Wed, 01 May 2024 07:28:52 GMT

←Older revision		Revision as of 07:28, 1 May 2024
Line 1:		Line 1:

	==NMR solution structure of SMO1, Sumo homologue in Caenorhabditis elegans==		==NMR solution structure of SMO1, Sumo homologue in Caenorhabditis elegans==
-	<StructureSection load='5xqm' size='340' side='right'caption='[[5xqm~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='5xqm' size='340' side='right'caption='[[5xqm]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5xqm]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XQM OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5XQM FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5xqm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XQM FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5xqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xqm OCA], [~~http~~://pdbe.org/5xqm PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5xqm RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5xqm PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5xqm ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=5xqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xqm OCA], [https://pdbe.org/5xqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xqm RCSB], [https://www.ebi.ac.uk/pdbsum/5xqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xqm ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/SUMO_CAEEL SUMO_CAEEL]] Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process (PubMed:11806825). Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction (PubMed:11806825, PubMed:25475837). Covalent attachment to its substrates requires prior activation by the E1 complex aos-1-uba-2 and linkage to the E2 enzyme ubc-9, and can be promoted by an E3 ligase such as gei-17 (PubMed:15107848, PubMed:16701625). Required for embryonic development, fertility, vulval morphogenesis and inhibition of vulval cell fates (PubMed:15466489, PubMed:15689373, PubMed:15990876, PubMed:24349540). Probably by sumoylating bet-1, prevents muscle myosin depletion in aging adults probably by preventing myoblast growth factor receptor egl-15 overexpression (PubMed:24285704). Plays a role in the attenuation of the let-60/ras pathway (PubMed:24349540, PubMed:24285704).<ref>PMID:11806825</ref> <ref>PMID:15107848</ref> <ref>PMID:15466489</ref> <ref>PMID:15689373</ref> <ref>PMID:15990876</ref> <ref>PMID:16701625</ref> <ref>PMID:24285704</ref> <ref>PMID:24349540</ref>	+	[https://www.uniprot.org/uniprot/SUMO_CAEEL SUMO_CAEEL] Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process (PubMed:11806825). Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction (PubMed:11806825, PubMed:25475837). Covalent attachment to its substrates requires prior activation by the E1 complex aos-1-uba-2 and linkage to the E2 enzyme ubc-9, and can be promoted by an E3 ligase such as gei-17 (PubMed:15107848, PubMed:16701625). Required for embryonic development, fertility, vulval morphogenesis and inhibition of vulval cell fates (PubMed:15466489, PubMed:15689373, PubMed:15990876, PubMed:24349540). Probably by sumoylating bet-1, prevents muscle myosin depletion in aging adults probably by preventing myoblast growth factor receptor egl-15 overexpression (PubMed:24285704). Plays a role in the attenuation of the let-60/ras pathway (PubMed:24349540, PubMed:24285704).<ref>PMID:11806825</ref> <ref>PMID:15107848</ref> <ref>PMID:15466489</ref> <ref>PMID:15689373</ref> <ref>PMID:15990876</ref> <ref>PMID:16701625</ref> <ref>PMID:24285704</ref> <ref>PMID:24349540</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	SUMO proteins are important post-translational modifiers involved in multiple cellular pathways in eukaryotes, especially during the different developmental stages in multicellular organisms. The nematode C. elegans is a well known model system for studying metazoan development and has a single SUMO homolog, SMO-1. Interestingly, SMO-1 modification is linked to embryogenesis and development in the nematode. However, high-resolution information about SMO-1 and the mechanism of its conjugation is lacking. In this work, we report the high-resolution three dimensional structure of SMO-1 solved by NMR spectroscopy. SMO-1 has flexible N-terminal and C-terminal tails on either side of a rigid beta-grasp folded core. While the sequence of SMO-1 is more similar to SUMO1, the electrostatic surface features of SMO-1 resemble more with SUMO2/3. SMO-1 can bind to typical SUMO Interacting Motifs (SIMs). SMO-1 can also conjugate to a typical SUMOylation consensus site as well as to its natural substrate HMR-1. Poly-SMO-1 chains were observed in-vitro even though SMO-1 lacks any consensus SUMOylation site. Typical deSUMOylation enzymes like Senp2 can cleave the poly-SMO-1 chains. Despite being a single gene, the SMO-1 structure allows it to function in a large repertoire of signaling pathways involving SUMO in C. elegans. Structural and functional features of SMO-1 studies described here will be useful to understand its role in development.	+
-		+
-	Structural and functional analysis of SMO-1, the SUMO homolog in Caenorhabditis elegans.,Surana P, Gowda CM, Tripathi V, Broday L, Das R PLoS One. 2017 Oct 18;12(10):e0186622. doi: 10.1371/journal.pone.0186622., eCollection 2017. PMID:29045470<ref>PMID:29045470</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 5xqm" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
Line 24:		Line 16:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Caenorhabditis elegans]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Das, R]]	+	[[Category: Das R]]
-	[[Category: Gowda~~, C M~~]]	+	[[Category: Gowda CM]]
-	[[Category: Surana, P]]	+	[[Category: Surana P]]
-	~~[[Category: Caenorhabditis elegan]]~~	+
-	~~[[Category: Signaling protein]]~~	+
-	~~[[Category: Solution structure]]~~	+
-	~~[[Category: Sumo homologue~~]]	+

OCA at 06:56, 14 October 2020

OCA — Wed, 14 Oct 2020 06:56:58 GMT

←Older revision		Revision as of 06:56, 14 October 2020
Line 1:		Line 1:

	==NMR solution structure of SMO1, Sumo homologue in Caenorhabditis elegans==		==NMR solution structure of SMO1, Sumo homologue in Caenorhabditis elegans==
-	<StructureSection load='5xqm' size='340' side='right' caption='[[5xqm]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='5xqm' size='340' side='right'caption='[[5xqm]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5xqm]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XQM OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5XQM FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5xqm]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XQM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5XQM 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=5xqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xqm OCA], [http://pdbe.org/5xqm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xqm RCSB], [http://www.ebi.ac.uk/pdbsum/5xqm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xqm ProSAT]</span></td></tr>	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5xqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xqm OCA], [http://pdbe.org/5xqm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xqm RCSB], [http://www.ebi.ac.uk/pdbsum/5xqm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xqm ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 17:
	</div>		</div>
	<div class="pdbe-citations 5xqm" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5xqm" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[SUMO 3D Structures\|SUMO 3D Structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Das, R]]		[[Category: Das, R]]
	[[Category: Gowda, C M]]		[[Category: Gowda, C M]]

OCA at 07:43, 8 November 2017

OCA — Wed, 08 Nov 2017 07:43:16 GMT

←Older revision		Revision as of 07:43, 8 November 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5xqm is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==NMR solution structure of SMO1, Sumo homologue in Caenorhabditis elegans==
		+	<StructureSection load='5xqm' size='340' side='right' caption='[[5xqm]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5xqm]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XQM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XQM 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=5xqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xqm OCA], [http://pdbe.org/5xqm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xqm RCSB], [http://www.ebi.ac.uk/pdbsum/5xqm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xqm ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SUMO_CAEEL SUMO_CAEEL]] Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process (PubMed:11806825). Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction (PubMed:11806825, PubMed:25475837). Covalent attachment to its substrates requires prior activation by the E1 complex aos-1-uba-2 and linkage to the E2 enzyme ubc-9, and can be promoted by an E3 ligase such as gei-17 (PubMed:15107848, PubMed:16701625). Required for embryonic development, fertility, vulval morphogenesis and inhibition of vulval cell fates (PubMed:15466489, PubMed:15689373, PubMed:15990876, PubMed:24349540). Probably by sumoylating bet-1, prevents muscle myosin depletion in aging adults probably by preventing myoblast growth factor receptor egl-15 overexpression (PubMed:24285704). Plays a role in the attenuation of the let-60/ras pathway (PubMed:24349540, PubMed:24285704).<ref>PMID:11806825</ref> <ref>PMID:15107848</ref> <ref>PMID:15466489</ref> <ref>PMID:15689373</ref> <ref>PMID:15990876</ref> <ref>PMID:16701625</ref> <ref>PMID:24285704</ref> <ref>PMID:24349540</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	SUMO proteins are important post-translational modifiers involved in multiple cellular pathways in eukaryotes, especially during the different developmental stages in multicellular organisms. The nematode C. elegans is a well known model system for studying metazoan development and has a single SUMO homolog, SMO-1. Interestingly, SMO-1 modification is linked to embryogenesis and development in the nematode. However, high-resolution information about SMO-1 and the mechanism of its conjugation is lacking. In this work, we report the high-resolution three dimensional structure of SMO-1 solved by NMR spectroscopy. SMO-1 has flexible N-terminal and C-terminal tails on either side of a rigid beta-grasp folded core. While the sequence of SMO-1 is more similar to SUMO1, the electrostatic surface features of SMO-1 resemble more with SUMO2/3. SMO-1 can bind to typical SUMO Interacting Motifs (SIMs). SMO-1 can also conjugate to a typical SUMOylation consensus site as well as to its natural substrate HMR-1. Poly-SMO-1 chains were observed in-vitro even though SMO-1 lacks any consensus SUMOylation site. Typical deSUMOylation enzymes like Senp2 can cleave the poly-SMO-1 chains. Despite being a single gene, the SMO-1 structure allows it to function in a large repertoire of signaling pathways involving SUMO in C. elegans. Structural and functional features of SMO-1 studies described here will be useful to understand its role in development.

-	~~Authors: Gowda~~, ~~C.M~~., Surana, P., ~~Das~~, R.	+	Structural and functional analysis of SMO-1, the SUMO homolog in Caenorhabditis elegans.,Surana P, Gowda CM, Tripathi V, Broday L, Das R PLoS One. 2017 Oct 18;12(10):e0186622. doi: 10.1371/journal.pone.0186622., eCollection 2017. PMID:29045470<ref>PMID:29045470</ref>

-	~~Description: NMR solution structure of SMO1~~, ~~Sumo homologue in Caenorhabditis elegans~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category~~: ~~Unreleased Structures]]~~	+	</div>
		+	<div class="pdbe-citations 5xqm" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Das, R]]		[[Category: Das, R]]
		+	[[Category: Gowda, C M]]
	[[Category: Surana, P]]		[[Category: Surana, P]]
-	[[Category: ~~Gowda, C.M~~]]	+	[[Category: Caenorhabditis elegan]]
		+	[[Category: Signaling protein]]
		+	[[Category: Solution structure]]
		+	[[Category: Sumo homologue]]

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

OCA — Wed, 27 Sep 2017 15:41:10 GMT

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

←Older revision

Revision as of 15:41, 27 September 2017

OCA: New page: '''Unreleased structure''' The entry 5xqm is ON HOLD until Paper Publication Authors: Gowda, C.M., Surana, P., Das, R. Description: NMR solution structure of SMO1, Sumo homologue in Ca...

OCA — Wed, 27 Sep 2017 15:41:09 GMT

New page: '''Unreleased structure''' The entry 5xqm is ON HOLD until Paper Publication Authors: Gowda, C.M., Surana, P., Das, R. Description: NMR solution structure of SMO1, Sumo homologue in Ca...

New page

'''Unreleased structure'''

The entry 5xqm is ON HOLD until Paper Publication

Authors: Gowda, C.M., Surana, P., Das, R.

Description: NMR solution structure of SMO1, Sumo homologue in Caenorhabditis elegans
[[Category: Unreleased Structures]]
[[Category: Das, R]]
[[Category: Surana, P]]
[[Category: Gowda, C.M]]