6grv

Cadmium(II) form of full-length metallothionein from Pseudomonas fluorescens Q2-87 (PflQ2 MT)

spinqualitylabelsall models 6grv Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6grv is a 1 chain structure with sequence from Pseudomonas fluorescens Q2-87. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Ligands: CD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MT_PSEFQ Metallothioneins are small proteins that have a high content of cysteine residues which allow them to bind heavy metal ions through clusters of thiolate bonds (PubMed:30191219). Preferentially, binds four Cd(2+) ions (PubMed:30191219). Also binds three Zn(2+) ions but with less affinity (PubMed:30191219). Required for long-term viability (PubMed:32793167). May play a role in the storage or sequestration of metals when present in excess (PubMed:32793167). Publication Abstract from PubMed Metallothioneins (MTs) are crucial players in metal-related physiological processes. They are characterized by a high cysteine content and unique metal binding properties resulting in specific metal-thiolate clusters formation. Here we present the first NMR solution structure of a Pseudomonas MT, PflQ2 MT, using the strain P. fluorescens Q2-87. It consists of a metal binding domain and an intrinsically disordered C-terminal tail, that was not observed in other MTs so far. While not influencing the structure or function of the metal binding domain, the tail contains a potential binding motif that might be important in so far undiscovered biological interactions. Unusual is the different metal binding capacity for three ZnII versus four CdII ions that results in two novel metal-cluster topologies. Nevertheless, the affinity for the fourth CdII ion is reduced due to transient coordination. PflQ2 MT contains an unusually large number of four histidine residues, of which only one is involved in metal ion binding. The three non-coordinating histidine residues influence neither the protein fold nor the stability in vitro. We demonstrate that reinstatement of a second coordinating histidine residue, observed for cyanobacterial MTs, in place of a non-coordinating residue in Pseudomonas MTs, decreases the kinetic lability of the cluster, while preserving the overall metal ion binding stability and the protein fold. Since high thermodynamic stability combined with high kinetic lability of metal binding are mechanistic features critical for the function of MTs, the observed replacement might be advantageous for Pseudomonas MTs with respect to metal ion handling in vivo. A histidine-rich Pseudomonas metallothionein with a disordered tail displays higher binding capacity for cadmium than zinc.,Habjanic J, Zerbe O, Freisinger E Metallomics. 2018 Sep 7. doi: 10.1039/c8mt00193f. PMID:30191219 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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