1OI0
CRYSTAL STRUCTURE OF AF2198, A JAB1/MPN DOMAIN PROTEIN FROM ARCHAEOGLOBUS FULGIDUS
Summary for 1OI0
Entry DOI | 10.2210/pdb1oi0/pdb |
Descriptor | HYPOTHETICAL PROTEIN AF2198, ZINC ION, TRIS-HYDROXYMETHYL-METHYL-AMMONIUM, ... (4 entities in total) |
Functional Keywords | proteasome, deubiquitination, archaea, hydrolase |
Biological source | ARCHAEOGLOBUS FULGIDUS |
Total number of polymer chains | 4 |
Total formula weight | 55969.62 |
Authors | Tran, H.J.T.T.,Allen, M.D.,Lowe, J.,Bycroft, M. (deposition date: 2003-06-04, release date: 2003-08-14, Last modification date: 2024-10-16) |
Primary citation | Tran, H.J.T.T.,Allen, M.D.,Lowe, J.,Bycroft, M. The Structure of the Jab1/Mpn Domain and its Implications for Proteasome Function Biochemistry, 42:11460-, 2003 Cited by PubMed Abstract: The 26S proteasome is responsible for the degradation of polyubiquitinated proteins. During this process the polyubiquitin chain is removed. The identity of the proteasomal component that is responsible for this activity has not been clear, as it contains no subunits that resemble known deubiquitinating enzymes. The Jab1/MPN domain is a widespread 120 amino acid protein module found in archaea, bacteria, and eukaryotes. In eukaryotes the Jab1/MPN domain is found in subunits of several multiprotein complexes including the proteasome. Recently it has been proposed that the Jab1/MPN domain of the proteasomal subunit Rpn11 is responsible for the removal of the polyubiquitin chain from substrate proteins. Here we report the crystal structure and characterization of AF2198, a Jab1/MPN domain protein from Archaeoglobolus fulgidus. The structure reveals a fold that resembles that of cytidine deaminase and places the Jab1/MPN domain in a superfamily of metal dependent hydrolases. PubMed: 14516197DOI: 10.1021/BI035033G PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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