Structural highlights
Function
[PSTS3_MYCTU] Part of the ABC transporter complex PstSACB involved in phosphate import (By similarity).
Publication Abstract from PubMed
Mycobacterium tuberculosis evades host immune responses by colonizing macrophages. Intraphagosomal M. tuberculosis is exposed to environmental stresses such as reactive oxygen and nitrogen intermediates as well as acid shock and inorganic phosphate (Pi) depletion. Experimental evidence suggests that expression levels of mycobacterial protein PstS3 (Rv0928) are significantly increased when M. tuberculosis bacilli are exposed to Pi starvation. Hence, PstS3 may be important for survival of Mtb in conditions where there is limited supply of Pi. We report here the structure of PstS3 from M. tuberculosis at 2.3-A resolution. The protein presents a structure typical for ABC phosphate transfer receptors. Comparison with its cognate receptor PstS1 showed a different pattern distribution of surface charges in proximity to the Pi recognition site, suggesting complementary roles of the two proteins in Pi uptake. Proteins 2014. (c) 2014 Wiley Periodicals, Inc.
Crystal structure of the Mycobacterium tuberculosis phosphate binding protein PstS3.,Ferraris DM, Spallek R, Oehlmann W, Singh M, Rizzi M Proteins. 2014 Mar 11. doi: 10.1002/prot.24548. PMID:24615888[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ferraris DM, Spallek R, Oehlmann W, Singh M, Rizzi M. Crystal structure of the Mycobacterium tuberculosis phosphate binding protein PstS3. Proteins. 2014 Mar 11. doi: 10.1002/prot.24548. PMID:24615888 doi:http://dx.doi.org/10.1002/prot.24548
