4A3P

Structure of USP15 DUSP-UBL deletion mutant

Summary for 4A3P

• Entry DOI: 10.2210/pdb4a3p/pdb
• Related: 1W6V 4A3O
• Descriptor: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 15, ACETATE ION, IODIDE ION, ... (4 entities in total)
• Functional Keywords: hydrolase
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 25330.28

Authors

Elliott, P.R.,Liu, H.,Pastok, M.W.,Grossmann, G.J.,Rigden, D.J.,Clague, M.J.,Urbe, S.,Barsukov, I.L. (deposition date: 2011-10-03, release date: 2011-11-16, Last modification date: 2023-12-20)

Primary citation

Elliott, P.R.,Liu, H.,Pastok, M.W.,Grossmann, G.J.,Rigden, D.J.,Clague, M.J.,Urbe, S.,Barsukov, I.L.
Structural Variability of the Ubiquitin Specific Protease Dusp-Ubl Double Domains.
FEBS Lett., 585:3385-, 2011

PubMed Abstract: USP4, 11 and 15 are three closely related paralogues of the ubiquitin specific protease (USP) family of deubiquitinating enzymes. The DUSP domain and the UBL domain in these proteins are juxtaposed which may provide a functional unit conferring specificity. We determined the structures of the USP15 DUSP-UBL double domain unit in monomeric and dimeric states. We then conducted comparative analysis of the structural and physical properties of all three DUSP-UBL units. We identified structural features that dictate different dispositions between constituent domains, which in turn may influence respective binding properties.

PubMed: 22001210
DOI: 10.1016/J.FEBSLET.2011.09.040

Experimental method

X-RAY DIFFRACTION (1.4 Å)