4.8 Article

Molecular mechanism underlying transport and allosteric inhibition of bicarbonate transporter SbtA

出版社

NATL ACAD SCIENCES
DOI: 10.1073/pnas.2101632118

关键词

bicarbonate transporter; CO2-concentrating mechanism; allosteric inhibition; structure; photosynthesis

资金

  1. National Key R&D Program of China [2019YFA0904602, 2018YFA0900602]
  2. National Natural Science Foundation of China [32025020, 31861130356]
  3. Chinese Academy of Sciences [XDB27020103]
  4. Shanghai Science and Technology Commission [19XD1424500]
  5. Newton Advanced Fellowship of The Royal Society [NAF/R1/180433]
  6. Royal Society [URF\R\180030, RGF\EA\181061, RGF\EA\180233]
  7. UK Biotechnology and Biological Sciences Research Council Grant [BB/R003890/1]

向作者/读者索取更多资源

The study presents the three-dimensional structures of the cyanobacterial Synechocystis sp. PCC 6803 SbtA-SbtB complex, revealing the functional unit as a trimer and the elevator mechanism adopted by SbtA for bicarbonate transport. The allosteric inhibition of SbtA by SbtB mainly occurs through the T-loop of SbtB, stabilizing the conformation with AMP molecules binding at the trimer interfaces. This unique regulatory mechanism of SbtA by SbtB highlights the importance of studying inorganic carbon uptake systems in CCM for potential modification of crop photosynthesis.
SbtA is a high-affinity, sodium-dependent bicarbonate transporter found in the cyanobacterial CO2-concentrating mechanism (CCM). SbtA forms a complex with SbtB, while SbtB allosterically regulates the transport activity of SbtA by binding with adenyl nucleotides. The underlying mechanism of transport and regulation of SbtA is largely unknown. In this study, we report the three-dimensional structures of the cyanobacterial Synechocystis sp. PCC 6803 SbtA-SbtB complex in both the presence and absence of HCO3- and/or AMP at 2.7 (A) over dot and 3.2 (A) over dot resolution. An analysis of the inward-facing state of the SbtA structure reveals the HCO3-/Na+ binding site, providing evidence for the functional unit as a trimer. A structural comparison found that SbtA adopts an elevator mechanism for bicarbonate transport. A structure-based analysis revealed that the allosteric inhibition of SbtA by SbtB occurs mainly through the T-loop of SbtB, which binds to both the core domain and the scaffold domain of SbtA and locks it in an inward-facing state. T-loop conformation is stabilized by the AMP molecules binding at the SbtB trimer interfaces and may be adjusted by other adenyl nucleotides. The unique regulatory mechanism of SbtA by SbtB makes it important to study inorganic carbon uptake systems in CCM, which can be used to modify photosynthesis in crops.

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