5ejj | pdb_00005ejj
Crystal structure of UfSP from C.elegans
Structural highlights
FunctionUFSP_CAEEL Thiol protease which recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ufm-1, a ubiquitin-like modifier protein bound to a number of target proteins (By similarity). Required, with oct-4, for the localization of a subset of 7 transmembrane domain odorant receptors, including odr-10, to the cilia of olfactory neurons AWA and AWC. Operates in aggregation behavior, and responses to oxygen levels.[UniProtKB:Q9NUQ7][1] [2] [3] Publication Abstract from PubMedUbiquitin-fold modifier 1 (Ufm1) specific protease (UfSP) is a novel cysteine protease that activates Ufm1 from its precursor by processing the C-terminus to expose the conserved Gly necessary for substrate conjugation and de-conjugates Ufm1 from the substrate. There are two forms: UfSP1 and UfSP2, the later with an additional domain at the N-terminus. Ufm1 and both the conjugating and deconjugating enzymes are highly conserved. However, in Caenorhabditis elegans there is one UfSP which has extra 136 residues at the N terminus compared to UfSP2. The crystal structure of cUfSP reveals that these additional residues display a MPN fold while the rest of the structure mimics that of UfSP2. The MPN domain does not have the metalloprotease activity found in some MPN-domain containing protein, rather it is required for the recognition and deufmylation of the substrate of cUfSP, UfBP1. In addition, the MPN domain is also required for localization to the endoplasmic reticulum. The MPN domain of Caenorhabditis elegans UfSP modulates both substrate recognition and deufmylation activity.,Ha BH, Kim KH, Yoo HM, Lee W, EunKyeong Kim E Biochem Biophys Res Commun. 2016 Aug 5;476(4):450-6. doi:, 10.1016/j.bbrc.2016.05.143. Epub 2016 May 28. PMID:27240952[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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