7agy

Structure of the N-domain of the K+/H+ antiporter subunit KhtT at pH 8.5

spinqualitylabelsall models 7agy, resolution 1.54Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7agy is a 2 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.54Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function KHTT_BACSU Required for activity of the potassium/proton antiporter KhtU (PubMed:14987767, PubMed:17679694). Involved in protection of the cell from methylglyoxal, a toxic by-product of glycolysis (PubMed:24330391). Publication Abstract from PubMed bis-(3',5')-cyclic diadenosine monophosphate (c-di-AMP) is a second messenger with roles in virulence, cell wall and biofilm formation, and surveillance of DNA integrity in many bacterial species, including pathogens. Strikingly, it has also been proposed to coordinate the activity of the components of K(+) homeostasis machinery, inhibiting K(+) import, and activating K(+) export. However, there is a lack of quantitative evidence supporting the direct functional impact of c-di-AMP on K(+) transporters. To gain a detailed understanding of the role of c-di-AMP on the activity of a component of the K(+) homeostasis machinery in B. subtilis, we have characterized the impact of c-di-AMP on the functional, biochemical, and physiological properties of KhtTU, a K(+)/H(+) antiporter composed of the membrane protein KhtU and the cytosolic protein KhtT. We have confirmed c-di-AMP binding to KhtT and determined the crystal structure of this complex. We have characterized in vitro the functional properties of KhtTU and KhtU alone and quantified the impact of c-di-AMP and of pH on their activity, demonstrating that c-di-AMP activates KhtTU and that pH increases its sensitivity to this nucleotide. Based on our functional and structural data, we were able to propose a mechanism for the activation of KhtTU by c-di-AMP. In addition, we have analyzed the impact of KhtTU in its native bacterium, providing a physiological context for the regulatory function of c-di-AMP and pH. Overall, we provide unique information that supports the proposal that c-di-AMP is a master regulator of K+ homeostasis machinery. c-di-AMP, a likely master regulator of bacterial K(+) homeostasis machinery, activates a K(+) exporter.,Cereija TB, Guerra JPL, Jorge JMP, Morais-Cabral JH Proc Natl Acad Sci U S A. 2021 Apr 6;118(14). pii: 2020653118. doi:, 10.1073/pnas.2020653118. PMID:33790011 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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