7pr5
Cocrystal of an RSL-N23H and sulfonato-thiacalix[4]arene - zinc complexCocrystal of an RSL-N23H and sulfonato-thiacalix[4]arene - zinc complex
Structural highlights
FunctionPublication Abstract from PubMedControlled protein assembly provides a means to generate biomaterials. Synthetic macrocycles such as the water-soluble sulfonato-calix[n]arenes are useful mediators of protein assembly. Sulfonato-thiacalix[4]arene (tsclx 4 ), with its metal-binding capacity, affords the potential for simultaneous macrocycle- and metal-mediated protein assembly. Here, we describe the tsclx 4 -/Zn-directed assembly of two proteins: cationic alpha-helical cytochrome c (cyt c) and neutral beta-propeller Ralstonia solanacearum lectin (RSL). Two co-crystal forms were obtained with cyt c, each involving multinuclear zinc sites supported by the cone conformation of tsclx 4 . The tsclx 4 /Zn cluster acted as an assembly node via both lysine encapsulation and metal-mediated protein-protein contacts. In the case of RSL, tsclx 4 adopted the 1,2-alternate conformation and supported a dinuclear zinc site with concomitant encapsulation and metal-binding of two histidine side chains. These results, together with the knowledge of thiacalixarene/metal nanoclusters, suggest promising applications for thiacalixarenes in biomaterials and MOF fabrication. Protein Frameworks with Thiacalixarene and Zinc.,Flood RJ, Ramberg KO, Mengel DB, Guagnini F, Crowley PB Cryst Growth Des. 2022 May 4;22(5):3271-3276. doi: 10.1021/acs.cgd.2c00108. Epub , 2022 Feb 22. PMID:35529063[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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