6ot8 | pdb_00006ot8

Bimetallic hexameric cage design 4 (BMC4) from cytochrome cb562

spinqualitylabelsall models 6ot8, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ot8 is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FE, HAE, HEC, ZN Related: 3m4b Gene: cybC ("Bacillus coli" Migula 1895) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [C562_ECOLX] Electron-transport protein of unknown function. Publication Abstract from PubMed Many proteins exist naturally as symmetrical homooligomers or homopolymers(1). The emergent structural and functional properties of such protein assemblies have inspired extensive efforts in biomolecular design(2-5). As synthesized by ribosomes, proteins are inherently asymmetric. Thus, they must acquire multiple surface patches that selectively associate to generate the different symmetry elements needed to form higher-order architectures(1,6)-a daunting task for protein design. Here we address this problem using an inorganic chemical approach, whereby multiple modes of protein-protein interactions and symmetry are simultaneously achieved by selective, 'one-pot' coordination of soft and hard metal ions. We show that a monomeric protein (protomer) appropriately modified with biologically inspired hydroxamate groups and zinc-binding motifs assembles through concurrent Fe(3+) and Zn(2+) coordination into discrete dodecameric and hexameric cages. Our cages closely resemble natural polyhedral protein architectures(7,8) and are, to our knowledge, unique among designed systems(9-13) in that they possess tightly packed shells devoid of large apertures. At the same time, they can assemble and disassemble in response to diverse stimuli, owing to their heterobimetallic construction on minimal interprotein-bonding footprints. With stoichiometries ranging from [2 Fe:9 Zn:6 protomers] to [8 Fe:21 Zn:12 protomers], these protein cages represent some of the compositionally most complex protein assemblies-or inorganic coordination complexes-obtained by design. Constructing protein polyhedra via orthogonal chemical interactions.,Golub E, Subramanian RH, Esselborn J, Alberstein RG, Bailey JB, Chiong JA, Yan X, Booth T, Baker TS, Tezcan FA Nature. 2020 Jan 22. pii: 10.1038/s41586-019-1928-2. doi:, 10.1038/s41586-019-1928-2. PMID:31969701 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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