5xqm
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==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. | ||
| - | + | 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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Das, R]] | [[Category: Das, R]] | ||
| + | [[Category: Gowda, C M]] | ||
[[Category: Surana, P]] | [[Category: Surana, P]] | ||
| - | [[Category: | + | [[Category: Caenorhabditis elegan]] |
| + | [[Category: Signaling protein]] | ||
| + | [[Category: Solution structure]] | ||
| + | [[Category: Sumo homologue]] | ||
Revision as of 07:43, 8 November 2017
NMR solution structure of SMO1, Sumo homologue in Caenorhabditis elegans
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