title: Structure of ubiquitin-fold modifier 1-specific protease UfSP2.
abstract: Ubiquitin-fold modifier 1 (Ufm1)-specific protease 2 (UfSP2) is a cysteine protease that is responsible for the release of Ufm1 from Ufm1-conjugated cellular proteins, as well as for the generation of mature Ufm1 from its precursor. The 2.6 Å resolution crystal structure of mouse UfSP2 reveals that it is composed of two domains. The C-terminal catalytic domain is similar to UfSP1 with Cys(294), Asp(418), His(420), Tyr(282), and a regulatory loop participating in catalysis. The novel N-terminal domain shows a unique structure and plays a role in the recognition of its cellular substrate C20orf116 and thus in the recruitment of UfSP2 to the endoplasmic reticulum, where C20orf116 predominantly localizes. Mutagenesis studies were carried out to provide the structural basis for understanding the loss of catalytic activity observed in a recently identified UfSP2 mutation that is associated with an autosomal dominant form of hip dysplasia.
authors.affiliation: Life Sciences Division, Korea Institute of Science and Technology, Seoul 136-791, Korea.
authors.forename: Byung Hak
authors.initials: BH
authors.lastname: Ha
authors.forename: Young Joo
authors.initials: YJ
authors.lastname: Jeon
authors.forename: Sang Chul
authors.initials: SC
authors.lastname: Shin
authors.forename: Kanako
authors.initials: K
authors.lastname: Tatsumi
authors.forename: Masaaki
authors.initials: M
authors.lastname: Komatsu
authors.forename: Keiji
authors.initials: K
authors.lastname: Tanaka
authors.forename: Christopher M
authors.initials: CM
authors.lastname: Watson
authors.forename: Gillian
authors.initials: G
authors.lastname: Wallis
authors.forename: Chin Ha
authors.initials: CH
authors.lastname: Chung
authors.forename: Eunice EunKyeong
authors.initials: EE
authors.lastname: Kim
mesh_terms: D000818:Animals; D002384:Catalysis; D018360:Crystallography, X-Ray; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000201:enzymology / Q000235:genetics; D006618:Hip Dislocation, Congenital / Q000201:enzymology / Q000235:genetics; D006801:Humans; D051379:Mice; D017434:Protein Structure, Tertiary; D011506:Proteins
chemical_list: D011506:Proteins; C513664:Ufm1 protein, mouse; D003546:Cysteine Endopeptidases; C518816:UfSP2 protein, mouse