Structural and biochemical characterization of a novel ZntB (CmaX) transporter protein from Pseudomonas aeruginosa

Stetsenko, Artem; Stehantsev, Pavlo; Dranenko, Natalia O; Gelfand, Mikhail S.; Guskov, Albert

doi:10.1016/j.ijbiomac.2021.06.130

Cited by 8 publications

(8 citation statements)

References 39 publications

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“…This is consistent with the widespread of negatively charged residues in Bpss1228, suggesting that it is also regulated by magnesium ions. Structural model of Bpss1228 was generated by the SWISS-MODEL server using P. aeruginosa CmaX as template (Stetsenko et al, 2021). This template was selected on the basis of the highest percentage of identity and sequence coverage of Bpss1228, and the best results on the geometry given by the CCP4 analysis.…”

Section: Resultsmentioning

confidence: 99%

Ion selectivity and gating behavior of the CorA-type channel Bpss1228

et al. 2022

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Magnesium is an essential element to sustain all forms of life. Total intracellular magnesium content is determined by the balance of magnesium influx and efflux. CorA is a divalent selective channel in the metal ion transport superfamily and is the major Mg2+ uptake pathway in prokaryotes and eukaryotic mitochondria. Previous studies have demonstrated that CorA showed distinct magnesium bound closed conformation and Mg2+-free states. In addition, CorA is regulated by cytoplasmic magnesium ions and its gating mechanism has been investigated by electron paramagnetic resonance technique and molecular dynamic simulations. Here, we report a study of the putative CorA-type channel Bpss1228 from Burkholderia pseudomallei, which has been shown to be significantly associated with pseudomallei infection. We expressed and purified the Bpss1228 in full-length. Subsequently, electrophysiological experiments further investigated the electrical characteristics of Bpss1228 and revealed that it was a strictly cation-selective channel. We also proved that Bpss1228 not only possessed magnesium-mediated regulatory property a remarkable ability to be modulated by magnesium ions. Finally, we observed the three-step gating behavior of Bpss1228 on planar lipid bilayer, and further proposed a synergistic gating mechanism by which CorA family channels control intracellular magnesium homeostasis.

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Section: Resultsmentioning

confidence: 99%

Ion selectivity and gating behavior of the CorA-type channel Bpss1228

et al. 2022

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“…ZntB belongs to the prokaryotic CorA family [ 111 , 112 ]. E. coli and P. aeruginosa ZntB transport multiple metal ions, including Zn 2+ , Co 2+ , Ni 2+ , and Cd 2+ [ 53 , 113 ]. ZntB forms homogeneous pentagonal structures that span the biological membrane, similar to other members of the CorA family.…”

Section: Zn 2+ Transport By Other Zn 2+ ...mentioning

confidence: 99%

“…ZntB forms homogeneous pentagonal structures that span the biological membrane, similar to other members of the CorA family. Each protomer consists of two TM helices and a large cytoplasmic domain [ 53 , 113 ]. ZnTB-mediated Zn 2+ transport is stimulated by a pH gradient across the biological membrane.…”

Section: Zn 2+ Transport By Other Zn 2+ ...mentioning

confidence: 99%

“…In contrast to bacterial YiiP and human ZnTs, ZntB does not seem to use an alternating access mechanism mediated by conformational transitions between IF and OF forms [ 53 ]. The cryo-EM structure of PaZntB is similar to that of EcZntB and T. maritima CorA, but with different helical arrangements [ 53 , 113 , 114 ]. PaZntB is capable of transporting Zn 2+ , Mg 2+ , Cd 2+ , Ni 2+ , and Co 2+ .…”

Section: Zn 2+ Transport By Other Zn 2+ ...mentioning

confidence: 99%

“…PaZntB is capable of transporting Zn 2+ , Mg 2+ , Cd 2+ , Ni 2+ , and Co 2+ . In contrast to other ZntBs, PaZntB is unlikely to use the proton motive force [ 53 , 113 ]. Thus, different mechanisms may operate among ZntBs from various bacterial species [ 53 , 111 , 113 , 115 ].…”

Section: Zn 2+ Transport By Other Zn 2+ ...mentioning

confidence: 99%

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Structures, Mechanisms, and Physiological Functions of Zinc Transporters in Different Biological Kingdoms

Bui,

Inaba

2024

IJMS

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Zinc transporters take up/release zinc ions (Zn2+) across biological membranes and maintain intracellular and intra-organellar Zn2+ homeostasis. Since this process requires a series of conformational changes in the transporters, detailed information about the structures of different reaction intermediates is required for a comprehensive understanding of their Zn2+ transport mechanisms. Recently, various Zn2+ transport systems have been identified in bacteria, yeasts, plants, and humans. Based on structural analyses of human ZnT7, human ZnT8, and bacterial YiiP, we propose updated models explaining their mechanisms of action to ensure efficient Zn2+ transport. We place particular focus on the mechanistic roles of the histidine-rich loop shared by several zinc transporters, which facilitates Zn2+ recruitment to the transmembrane Zn2+-binding site. This review provides an extensive overview of the structures, mechanisms, and physiological functions of zinc transporters in different biological kingdoms.

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