Abstract
Using energy and density guided Rosetta refinement to improve molecular replacement, we have determined the crystal structure of the protease (PR) encoded by xenotropic murine leukemia virus-related virus (XMRV). Despite overall similarity of XMRV PR to other retropepsins, the topology of its dimer interface more closely resembles the monomeric, pepsin-like enzymes. Thus, XMRV PR may represent a distinct evolutionary branch of the family of aspartic proteases.
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