Structural highlights
Publication Abstract from PubMed
The obligate intracellular, gram-negative bacterium Rickettsia is the causative agent of spotted fevers and typhus in humans. Surface cell antigen (sca) proteins surround these bacteria. We recently reported the colocalization of one of these proteins, sca4, with vinculin in cells at sites of focal adhesions and demonstrated that two vinculin binding sites directed the sca4/vinculin interaction. Here we report the 2.2 A crystal structure of the conserved N-terminal 38 kDa domain of sca4 from Rickettsia rickettsii. The structure reveals two subdomains. The first is an all-helical domain that is folded in a fashion similar to the dimeric assembly chaperone for rubisco, namely RbcX. The following and highly conserved beta-strand domain lacks significant structural similarity with other known structures and to the best of our knowledge represents a new protein fold.
Crystal structure of the N-terminal domains of the surface cell antigen 4 of Rickettsia.,Lee JH, Vonrhein C, Bricogne G, Izard T Protein Sci. 2013 Jul 31. doi: 10.1002/pro.2322. PMID:23904352[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lee JH, Vonrhein C, Bricogne G, Izard T. Crystal structure of the N-terminal domains of the surface cell antigen 4 of Rickettsia. Protein Sci. 2013 Jul 31. doi: 10.1002/pro.2322. PMID:23904352 doi:10.1002/pro.2322
