Ontology highlight
ABSTRACT:
SUBMITTER: Ambroggio XI
PROVIDER: S-EPMC300881 | biostudies-literature | 2004 Jan
REPOSITORIES: biostudies-literature
Ambroggio Xavier I XI Rees Douglas C DC Deshaies Raymond J RJ
PLoS biology 20031124 1
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 tha ...[more]