Crystal structure of XMRV protease differs from the structures of other retropepsins - PubMed (original) (raw)

Crystal structure of XMRV protease differs from the structures of other retropepsins

Mi Li et al. Nat Struct Mol Biol. 2011 Feb.

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.

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Figures

Figure 1

The structure of XMRV PR and a comparison with the fold of typical retroviral proteases. a) A dimer of XMRV PR in cartoon representation, with the two monomers colored cyan and blue and the catalytic aspartates shown as sticks. b) A superposition based on Cα coordinates of XMRV PR (cyan) and the apoenzyme of HIV-1 PR (green, PDB code 3hvp), shown in cartoon representation. c) Structure-based sequence alignment of the XMRV, HIV-1, and EIAV PRs, as well as Ddi1 RP. Secondary structure elements and residue numbers are marked above for XMRV PR and below for HIV-1 PR. Residues identical in all four enzymes are boxed. Panels a and b were prepared with PyMol.

Figure 2

Dimer interface regions in aspartic proteases. Strands belonging to the N-terminal regions of the molecules (or domains in pepsin) are blue, and the C-terminal regions are red. a) XMRV PR; b) HIV-1 PR; c) Ddi1 RP; d) pepsin.

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Crystal structure of XMRV protease differs from the structures of other retropepsins - PubMed (original) (raw)