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5XQM

NMR solution structure of SMO1, Sumo homologue in Caenorhabditis elegans

Summary for 5XQM
Entry DOI10.2210/pdb5xqm/pdb
NMR InformationBMRB: 36096
DescriptorSmall ubiquitin-related modifier (1 entity in total)
Functional Keywordssolution structure, caenorhabditis elegans, sumo homologue, signaling protein
Biological sourceCaenorhabditis elegans
Cellular locationCytoplasm : P55853
Total number of polymer chains1
Total formula weight11048.22
Authors
Gowda, C.M.,Surana, P.,Das, R. (deposition date: 2017-06-07, release date: 2017-11-08, Last modification date: 2024-05-01)
Primary citationSurana, P.,Gowda, C.M.,Tripathi, V.,Broday, L.,Das, R.
Structural and functional analysis of SMO-1, the SUMO homolog in Caenorhabditis elegans
PLoS ONE, 12:e0186622-e0186622, 2017
Cited by
PubMed Abstract: 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.
PubMed: 29045470
DOI: 10.1371/journal.pone.0186622
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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