Crystal structure related to rheumatic autoimmune diseases
James Sacchettini group (Texas A&M University)
James Sacchettini's laboratory at Texas A&M University
recently solved several structures, including the structure of Rsr, an
ortholog of the antigenic Ro protein. Ro proteins are a class of antigenic
ribonucleo-proteins associated with rheumatic autoimmune diseases in humans.
Ro is suggested to play a role in RNA quality control and has also been
implicated in cell survival following UV damage. The 1.9-Å crystal
structure of this prokaryotic ortholog, Rsr from D. raiodurans, was
determined using GM/CA-CAT beamtime. It is composed of an N-terminal domain
consisting of 18 α-helices and a C-terminal domain of a β-sheet
(blue) sandwiched between sets of helices. Residues in the C-terminal domain
coordinate a calcium ion (yellow).
Figure: 1.9-Å crystal structure of D. radiodurans Rsr.
Ramesh, A, Savva, CG, Holzenburg, A, Sacchettini, JC. Crystal Structure of
Rsr, an Ortholog of the Antigenic Ro Protein, Links Conformational
Flexibility to RNA Binding Activity, J. Biol. Chem. 282 (20), 14960-14967
(2007). DOI: 10.1074/jbc.M611163200.