3OQC

Ubiquitin-fold modifier 1 Specific Protease, UfSP2

Summary for 3OQC

• Entry DOI: 10.2210/pdb3oqc/pdb
• Descriptor: Ufm1-specific protease 2 (2 entities in total)
• Functional Keywords: dph motif cys protease, hydrolase
• Biological source: Mus musculus (mouse)
• Cellular location: Cytoplasm: Q99K23
• Total number of polymer chains: 2
• Total formula weight: 109348.38

Authors

Ha, B.H.,Chung, C.H.,Kim, E.E. (deposition date: 2010-09-02, release date: 2011-01-12, Last modification date: 2024-03-20)

Primary citation

Ha, B.H.,Jeon, Y.J.,Shin, S.C.,Tatsumi, K.,Komatsu, M.,Tanaka, K.,Watson, C.M.,Wallis, G.,Chung, C.H.,Kim, E.E.
Structure of ubiquitin-fold modifier 1-specific protease UfSP2
J.Biol.Chem., 286:10248-10257, 2011

PubMed 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.

PubMed: 21228277
DOI: 10.1074/jbc.M110.172171

Experimental method

X-RAY DIFFRACTION (2.6 Å)