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2J7Q

Crystal structure of the ubiquitin-specific protease encoded by murine cytomegalovirus tegument protein M48 in complex with a ubquitin-based suicide substrate

Summary for 2J7Q
Entry DOI10.2210/pdb2j7q/pdb
Related1C3T 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
DescriptorMCMV TEGUMENT PROTEIN M48 ENCODED UBIQUITIN- SPECIFIC PROTEASE, M48USP, UBIQUITIN, MAGNESIUM ION, ... (8 entities in total)
Functional Keywordsherpesviridae, nuclear protein, covalent enzyme-ligand complex, deubiquitinating enzyme, hydrolase, papain-like fold, cysteine protease
Biological sourceMURINE CYTOMEGALOVIRUS
More
Total number of polymer chains4
Total formula weight68996.69
Authors
Schlieker, C.,Weihofen, W.A.,Frijns, E.,Kattenhorn, L.M.,Gaudet, R.,Ploegh, H.L. (deposition date: 2006-10-16, release date: 2007-03-20, Last modification date: 2023-11-15)
Primary citationSchlieker, C.,Weihofen, W.A.,Frijns, E.,Kattenhorn, L.M.,Gaudet, R.,Ploegh, H.L.
Structure of a Herpesvirus-Encoded Cysteine Protease Reveals a Unique Class of Deubiquitinating Enzymes
Mol.Cell, 25:677-, 2007
Cited by
PubMed Abstract: 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.
PubMed: 17349955
DOI: 10.1016/J.MOLCEL.2007.01.033
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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