9ppn

Cu-bound structure of the H77C variant of TriCyt2

spinqualitylabelsall models 9ppn, resolution 1.87Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9ppn is a 3 chain structure with sequence from Escherichia coli BL21(DE3). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.87Å Ligands: CU Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C562_ECOLX Electron-transport protein of unknown function. Publication Abstract from PubMed The design of proteins with selective metal-binding properties to accommodate distinct metal ions remains a challenge in the field of artificial metalloprotein design. Here, we report our design approach to incorporate heterodinuclear metal coordination motifs along the interface of a trimeric protein assembly, termed (H77C)TriCyt2, that enables the selective binding of the post-transition metal ion Bi(III) and a first-row transition metal ion (M(II)). The coordination sites are composed of soft tris-Cys donors and intermediate/hard tris-His centers that are placed proximally to one another within the highly stable, preorganized trimeric architecture of (H77C)TriCyt2 to allow for the formation of a heterodinuclear center. We obtained crystal structures (at 2.5 A resolution or better) of the (H77C)TriCyt2 trimer complexed with a first-row transition metal (Mn(II), Co(II), Ni(II), Cu(II), or Zn(II)) that binds at the tris-His site, and a (H77C)TriCyt2 structure complexed with Bi(III) at the tris-Cys site, thereby confirming the selectivity of metal binding motifs as designed. Additionally, we obtained the crystal structures of BiCo, BiNi, and BiZn heterodinuclear proteins, and demonstrated through solution experiments that the trimeric state of (H77C)TriCyt2 is maintained upon the concomitant addition of Bi(III) and various M(II) species. Structural analyses of the mononuclear and heterodinuclear (H77C)TriCyt2 structures further revealed different Bi(III) binding geometries in each case, which indicated that the preferential coordination geometries of the transition metal ions can influence the Bi(III) coordination geometry and that subtle structural changes within the protein structure may promote or disfavor Bi(III) binding. Design of a protein scaffold with a selective, Bi-containing heterodinuclear metal coordination motif.,Eng VH, Gascon M, Kakkis A, Tezcan FA J Inorg Biochem. 2025 Oct 7;274:113104. doi: 10.1016/j.jinorgbio.2025.113104. PMID:41072111 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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