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Crystal structure of the Mycobacterium tuberculosis phosphate binding protein PstS3

Davide M Ferraris1, Ralf Spallek, Wulf Oehlmann

  • 1Department of Pharmaceutical Sciences, Università del Piemonte Orientale "A. Avogadro,", Largo Donegani 2, 28100, Novara, Italy.

Proteins
|March 12, 2014
PubMed

Insights

Mycobacterium tuberculosis uses protein PstS3 to survive phosphate starvation within macrophages. Its structure reveals a phosphate transporter, suggesting a key role in inorganic phosphate uptake for Mtb survival.

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Mycobacterium tuberculosis (Mtb) survives within host macrophages, facing environmental stresses.
  • Phosphate (Pi) depletion is a key stressor, leading to increased expression of the Mtb protein PstS3.
  • PstS3 is hypothesized to be crucial for Mtb survival during Pi starvation.

Purpose of the Study:

  • To determine the structure of Mycobacterium tuberculosis PstS3.
  • To understand the role of PstS3 in inorganic phosphate uptake and Mtb survival.

Main Methods:

  • X-ray crystallography was used to determine the PstS3 structure at 2.3-Å resolution.
  • Structural comparison with the related PstS1 protein was performed.

Main Results:

  • The structure of PstS3 was elucidated, revealing it as an ABC phosphate transfer receptor.
  • PstS3 exhibits distinct surface charge distribution near the Pi binding site compared to PstS1.
  • This suggests complementary functions in inorganic phosphate acquisition.

Conclusions:

  • PstS3 is a structural homolog of phosphate ABC transporters.
  • The structural differences between PstS3 and PstS1 indicate specialized roles in inorganic phosphate uptake.
  • PstS3 likely plays a significant role in Mtb's adaptation to low-phosphate environments within the host.
Keywords:
Pst systembacterial survivalbinding affinityphosphate depletionprotein refolding and crystallizationthermal shift assaytuberculosistwo-component system

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