XMRV protease -crystal structure differs from other retropepsins

[Guest guest]

http://bit.ly/eSDg8f

nature Structural & molecular biology

Brief Communication

Crystal structure of XMRV

protease differs from the

structures of other retropepsins

Mi Li, DiMaio, Dongwen Zhou, Alla

Gustchina, Jacek Lubkowski, Zbigniew

Dauter, Baker, &

Wlodawer

Nature Structural & Molecular Biology

(2011)

doi:10.1038/nsmb.1964

Received 29 July 2010

Accepted 29 October 2010

Published online 23 January 2011

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.

````````

The Supplementary Text and Figures (3M)

The Supplementary Figures 1–7, Supplementary

Tables 1 and 2, and Supplementary Methods can be

found for free at: http://bit.ly/gz7AQE

The full article can be bought at: http://bit.ly/fDzzhU

(I hold me highly recommended)