1r5x

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(New page: 200px<br /><applet load="1r5x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r5x, resolution 2.30&Aring;" /> '''JAMM: A Metalloprote...)
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Revision as of 20:04, 24 November 2007

Image:1r5x.gif

1r5x, resolution 2.30Å

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

Overview

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(n)HS/THX(7)SXXD, 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.

About this Structure

1R5X is a Single protein structure of sequence from Archaeoglobus fulgidus dsm 4304 with ZN as ligand. Full crystallographic information is available from OCA.

Reference

JAMM: a metalloprotease-like zinc site in the proteasome and signalosome., Ambroggio XI, Rees DC, Deshaies RJ, PLoS Biol. 2004 Jan;2(1):E2. Epub 2003 Nov 24. PMID:14737182

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