4LVQ
Crystal structure of the M. tuberculosis phosphate binding protein PstS3
Summary for 4LVQ
| Entry DOI | 10.2210/pdb4lvq/pdb |
| Descriptor | Phosphate-binding protein PstS 3, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | phosphate binding protein, extracellular, transport protein |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 2 |
| Total formula weight | 77809.43 |
| Authors | Ferraris, D.M.,Rizzi, M. (deposition date: 2013-07-26, release date: 2014-03-26, Last modification date: 2024-11-27) |
| Primary citation | Ferraris, D.M.,Spallek, R.,Oehlmann, W.,Singh, M.,Rizzi, M. Crystal structure of the Mycobacterium tuberculosis phosphate binding protein PstS3. Proteins, 82:2268-2274, 2014 Cited by PubMed Abstract: 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-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. PubMed: 24615888DOI: 10.1002/prot.24548 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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