3NR6
Crystal structure of xenotropic murine leukemia virus-related virus (XMRV) protease
Summary for 3NR6
| Entry DOI | 10.2210/pdb3nr6/pdb |
| Related | 2FMB 2HVP 2I1A 2RSP 4FIV |
| Descriptor | Protease p14, POTASSIUM ION, PHOSPHATE ION, ... (4 entities in total) |
| Functional Keywords | dimer, protease, hydrolase-inhibitor complex, hydrolase/inhibitor |
| Biological source | Xenotropic MuLV-related virus VP62 |
| Cellular location | Gag-Pol polyprotein: Host cell membrane ; Lipid-anchor . Matrix protein p15: Virion . Capsid protein p30: Virion . Nucleocapsid protein p10: Virion : A1Z651 |
| Total number of polymer chains | 2 |
| Total formula weight | 28824.65 |
| Authors | Lubkowski, J.,Li, M.,Gustchina, A.,Zhou, D.,Dauter, Z.,Wlodawer, A. (deposition date: 2010-06-30, release date: 2011-02-02, Last modification date: 2024-04-03) |
| Primary citation | Li, M.,Dimaio, F.,Zhou, D.,Gustchina, A.,Lubkowski, J.,Dauter, Z.,Baker, D.,Wlodawer, A. Crystal structure of XMRV protease differs from the structures of other retropepsins. Nat.Struct.Mol.Biol., 18:227-229, 2011 Cited by PubMed Abstract: Using energy and density guided Rosetta refinement to improve molecular replacement, we determined the crystal structure of the protease encoded by xenotropic murine leukemia virus-related virus (XMRV). Despite overall similarity of XMRV protease to other retropepsins, the topology of its dimer interface more closely resembles those of the monomeric, pepsin-like enzymes. Thus, XMRV protease may represent a distinct branch of the aspartic protease family. PubMed: 21258323DOI: 10.1038/nsmb.1964 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.97 Å) |
Structure validation
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