ArticleProtein science : a publication of the Protein Society2009
Structure and electrostatic property of cytoplasmic domain of ZntB transporter.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 25 citations in OpenAlex.
- The C-terminal activating domain promotes pannexin 1 channel opening.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- CHARMM at 45: Enhancements in Accessibility, Functionality, and Speed.The journal of physical chemistry. B · 2024Review
- The C-terminal activating domain promotes Panx1 channel opening.bioRxiv : the preprint server for biology · 2024Article
- Structures, Mechanisms, and Physiological Functions of Zinc Transporters in Different Biological Kingdoms.International journal of molecular sciences · 2024Review
- Ion selectivity and gating behavior of the CorA-type channel Bpss1228.Frontiers in chemistry · 2022Article
- Cation permeability in CorA family of proteins.Scientific reports · 2020Article
- The structural basis of proton driven zinc transport by ZntB.Nature communications · 2017Article
- X-ray crystallography and isothermal titration calorimetry studies of the Salmonella zinc transporter ZntB.Structure (London, England : 1993) · 2011Article
- Co2+ selectivity of Thermotoga maritima CorA and its inability to regulate Mg2+ homeostasis present a new class of CorA proteins.The Journal of biological chemistry · 2011Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
ZntB is the distant homolog of CorA Mg(2+) transporter within the metal ion transporter superfamily. It was early reported that the ZntB from Salmonella typhimurium facilitated efflux of Zn(2+) and Cd(2+), but not Mg(2+). Here, we report the 1.90 A crystal structure of the intracellular domain of ZntB from Vibrio parahemolyticus. The domain forms a funnel-shaped homopentamer that is similar to the full-length CorA from Thermatoga maritima, but differs from two previously reported dimeric structures of truncated CorA intracellular domains. However, no Zn(2+) or Cd(2+) binding sites were identified in the high-resolution structure. Instead, 25 well-defined Cl(-) ions were observed and some of these binding sites are highly conserved within the ZntB family. Continuum electrostatics calculations suggest that the central pore of the funnel is highly attractive for cations, especially divalents. The presence of the bound Cl(-) ions increases the stability of cations along the pore suggesting they could be important in enhancing cation transport.
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Registered trials
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