Crystal structure of XMRV protease differs from the structures of other retropepsins.
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.
Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, Maryland, USA.
Mi
M
Li
Frank
F
Dimaio
Dongwen
D
Zhou
Alla
A
Gustchina
Jacek
J
Lubkowski
Zbigniew
Z
Dauter
David
D
Baker
Alexander
A
Wlodawer
D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000737:chemistry*; D055503:Protein Multimerization; D014764:Viral Proteins / Q000737:chemistry*; D058008:Xenotropic murine leukemia virus-related virus / Q000737:chemistry / Q000201:enzymology*
D014764:Viral Proteins; D010447:Peptide Hydrolases
Retrovirology. 2010 Feb 15;7:10
20156349
PLoS One. 2010 Apr 01;5(4):e9948
20376347
Science. 1989 Aug 11;245(4918):616-21
2548279
Proc Natl Acad Sci U S A. 2009 Sep 22;106(38):16351-6
19805305
Proc Natl Acad Sci U S A. 1985 Mar;82(6):1618-22
3885215
Nat Struct Biol. 1999 Sep;6(9):868-75
10467100
J Mol Biol. 2006 Dec 1;364(3):376-87
17010377
Genome Biol. 2002;3(4):REVIEWS3006
11983066
Science. 2009 Oct 23;326(5952):585-9
19815723
J Mol Biol. 2008 Aug 1;381(1):141-9
18597783
Annu Rev Biophys Biomol Struct. 1998;27:249-84
9646869
J Mol Biol. 2009 Sep 11;392(1):181-90
19596339
Annu Rev Biochem. 1993;62:543-85
8352596
Cell Cycle. 2006 Mar;5(5):463-4
16479175
Nature. 1989 Feb 9;337(6207):576-9
2536902
Nature. 1978 Feb 16;271(5646):618-21
24179