Crystal structure of the Mycobacterium tuberculosis phosphate binding protein PstS3. Issue 9 (24th March 2014)

• Record Type: Journal Article
• Authors: Ferraris, Davide M.; Spallek, Ralf; Oehlmann, Wulf; Singh, Mahavir; Rizzi, Menico
• Is Part Of: Proteins. Volume 82:Issue 9(2014)
• Page Start: 2268
• Page End: 2274
• Publication Date: 2014-03-24
• Subjects: Proteins -- Periodicals; Proteins -- Periodicals; 572.6
• DOI: 10.1002/prot.24548
• Languages: English
• ISSNs: 0887-3585

Abstract

<abstract abstract-type="main"> <title>ABSTRACT</title> <p> <italic>Mycobacterium tuberculosis</italic> evades host immune responses by colonizing macrophages. Intraphagosomal <italic>M. tuberculosis</italic> 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 <italic>M. tuberculosis</italic> 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 <italic>M. tuberculosis</italic> at 2.3‐Å 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; 82:2268–2274. © 2014 Wiley Periodicals, Inc.</p> </abstract>