1vjv
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Protein Summary
UBP6 from Saccharomyces cerevisiae is a cysteine peptidase (EC:3.1.2.15) and contains two domains - an N-terminal ubiquitin (Ub) domain and a C-terminal catalytic domain. The crystal structure corresponds to the catalytic domain of UBP6 which belongs to the C.19.079 family of MEROPS database. The cysteine peptidase deubiquitinating enzyme (DUBs) family can be further subdivided into four subfamilies namely the Ub-specific protease (USP), Ub C-terminal hydrolase (UCH), Otubain protease (OTU) and Machado-Joseph disease protease (MJD). UBP6 belongs to the USP subfamily which is the largest and most diverse among the DUBs. The catalytic triad of this cysteine peptidase is comprised of residues C118, H447 and N465. N113 is also in the vicinity of the active site. In addition the UBP6 protein has a degraded zinc ribbon motif (unlikely to bind zinc in UBP6) inserted between structural elements of the peptidase core. The presence of the zinc ribbon was predicted by Krishna and Grishin (2004) based on the structure of the human protein HAUSP {ref Cell cycle 2004}. The structure of the homologous USP8 contains an intact zinc-binding ribbon. Crystallographic packing indicates UBP6 to be a monomer.
Ligand Summary
References
Reviews
References
No references found.
