| Structural highlights
2j7q is a 4 chain structure with sequence from Human and Muhv1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , |
| NonStd Res: | |
| Related: | 1c3t, 1d3z, 1f9j, 1fxt, 1g6j, 1gjz, 1nbf, 1ogw, 1q5w, 1s1q, 1sif, 1tbe, 1ubi, 1ubq, 1xd3, 1xqq, 1yx5, 1yx6, 1zgu, 2ayo, 2bgf, 2fcm, 2fcn, 2fcq, 2fcs, 2fuh, 2g45, 2gbk, 2gbm, 2gbn |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
All members of the herpesviridae contain within their large tegument protein a cysteine protease module that displays deubiquitinating activity. We report the crystal structure of the cysteine protease domain of murine cytomegalovirus M48 (M48(USP)) in a complex with a ubiquitin (Ub)-based suicide substrate. M48(USP) adopts a papain-like fold, with the active-site cysteine forming a thioether linkage to the suicide substrate. The Ub core participates in an extensive hydrophobic interaction with an exposed beta hairpin loop of M48(USP). This Ub binding mode contributes to Ub specificity and is distinct from that observed in other deubiquitinating enzymes. Both the arrangement of active-site residues and the architecture of the interface with Ub lead us to classify this domain as the founding member of a previously unknown class of deubiquitinating enzymes.
Structure of a herpesvirus-encoded cysteine protease reveals a unique class of deubiquitinating enzymes.,Schlieker C, Weihofen WA, Frijns E, Kattenhorn LM, Gaudet R, Ploegh HL Mol Cell. 2007 Mar 9;25(5):677-87. PMID:17349955[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schlieker C, Weihofen WA, Frijns E, Kattenhorn LM, Gaudet R, Ploegh HL. Structure of a herpesvirus-encoded cysteine protease reveals a unique class of deubiquitinating enzymes. Mol Cell. 2007 Mar 9;25(5):677-87. PMID:17349955 doi:10.1016/j.molcel.2007.01.033
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