JAMM: A Metalloprotease-Like Zinc Site in the Proteasome and Signalosome

Ambroggio, Xavier I.; Rees, Douglas C.; Deshaies, Raymond J.

doi:10.1371/journal.pbio.0020002

JAMM: A Metalloprotease-Like Zinc Site in the Proteasome and Signalosome

Journal Article · Mon Nov 24 04:00:00 EST 2003 · PLoS Biology (Online)

DOI:https://doi.org/10.1371/journal.pbio.0020002· OSTI ID:1627129

Ambroggio, Xavier I. ^[1]; Rees, Douglas C. ^[2]; Deshaies, Raymond J. ^[3]

California Institute of Technology (CalTech), Pasadena, CA (United States). Division of Biology; DOE/OSTI
California Institute of Technology (CalTech), Pasadena, CA (United States). Division of Chemistry and Chemical Engineering; Howard Hughes Medical Inst., Chevy Chase, MD (United States)
California Institute of Technology (CalTech), Pasadena, CA (United States). Division of Biology; Howard Hughes Medical Inst., Chevy Chase, MD (United States)

The JAMM (JAB1/MPN/Mov34 metalloenzyme) motif in Rpn₁₁ and Csn₅ underlies isopeptidase activities intrinsic to the proteasome and signalosome, respectively. We show here that the archaebacterial protein AfJAMM possesses the key features of a zinc metalloprotease, yet with a distinct fold. The histidine and aspartic acid of the conserved EX_nHS/ THX₇SXXD motif coordinate a zinc, whereas the glutamic acid hydrogen-bonds an aqua ligand. By analogy to the active site of thermolysin, we predict that the glutamic acid serves as an acid-base catalyst and the second serine stabilizes a tetrahedral intermediate. Mutagenesis of Csn₅ confirms these residues are required for Nedd8 isopeptidase activity. The active site-like architecture specified by the JAMM motif motivates structure-based approaches to the study of JAMM domain proteins and the development of therapeutic proteasome and signalosome inhibitors.

View Accepted Manuscript (DOE)

Research Organization:: SLAC National Accelerator Laboratory, Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL); Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States). Advanced Light Source (ALS)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER); USDOE Office of Science (SC), Basic Energy Sciences (BES). Materials Sciences & Engineering Division

Grant/Contract Number:: AC02-76SF00515; AC03-76SF00098

OSTI ID:: 1627129

Journal Information:: PLoS Biology (Online), Journal Name: PLoS Biology (Online) Journal Issue: 1 Vol. 2; ISSN 1545-7885

Publisher:: Public Library of ScienceCopyright Statement

Country of Publication:: United States

Language:: English

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The ESCRT-III-Interacting Deubiquitinating Enzyme AMSH3 is Essential for Degradation of Ubiquitinated Membrane Proteins in Arabidopsis thaliana Katsiarimpa, Anthi; Muñoz, Alfonso; Kalinowska, Kamila Plant and Cell Physiology, Vol. 55, Issue 4 https://doi.org/10.1093/pcp/pcu019	journal	February 2014
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Zinc: A Necessary Ion for Mammalian Sperm Fertilization Competency Kerns, Karl; Zigo, Michal; Sutovsky, Peter International Journal of Molecular Sciences https://doi.org/10.20944/preprints201811.0425.v1	journal	January 2018
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Yeast as a tool to select inhibitors of the cullin deneddylating enzyme Csn5 Cirigliano, Angela; Stirpe, Alessandro; Menta, Sergio Taylor & Francis https://doi.org/10.6084/m9.figshare.3204460.v1	text	January 2016
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