YIIPYouth International Internship Program (Canada)
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References in periodicals archive ?
Since metallochaperones and their targets share a metallochaperone domain, a zinc chaperone that binds to YiiP and transfers zinc might exist.
In the crystal structure of YiiP, the two positively charged protein surfaces of the CTD interface are held by four [Zn.sup.2+] ions [39, 45].
In general, CTD structures without TMDs are distinct from the full-length structure of YiiP. Therefore, the action/role of the CTD is still controversial.
Using the purified YiiP protein, zinc efflux occurs via a [Zn.sup.2+]/[H.sup.+] antiporter [44].
Fu, "Structure of the zinc transporter YiiP," Science, vol.
Fu, "Thermodynamic studies of the mechanism of metal binding to the Escherichia coli zinc transporter YiiP," The Journal of Biological Chemistry, vol.
Fu, "Structural basis for autoregulation of the zinc transporter YiiP," Nature Structural & Molecular Biology, vol.