7BAE

Crystal structure of PAFB

Summary for 7BAE

• Entry DOI: 10.2210/pdb7bae/pdb
• Related: 2NC2
• Descriptor: Antifungal protein (2 entities in total)
• Functional Keywords: penicillium chrysogenum antifungal protein b, calix[n]arene, porous framework, zinc, antifungal protein
• Biological source: Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255)
• Total number of polymer chains: 1
• Total formula weight: 6516.39

Authors

Guagnini, F.,Huber, A.,Alex, J.M.,Marx, F.,Crowley, P.B. (deposition date: 2020-12-15, release date: 2021-03-17, Last modification date: 2024-01-31)

Primary citation

Guagnini, F.,Huber, A.,Alex, J.M.,Marx, F.,Crowley, P.B.
Porous assembly of an antifungal protein mediated by zinc and sulfonato-calix[8]arene.
J.Struct.Biol., 213:107711-107711, 2021

PubMed Abstract: Controlled protein assembly holds great potential in the fabrication of biohybrid materials. However, the structural diversity and complexity of proteins present an obstacle to controlled assembly. Supramolecular chemistry is a possible solution as it offers tools to mediate self-assembly with molecular precision. This paper deals with the calixarene- and zinc-mediated assembly and crystallization of the histidine-rich Penicillium chrysogenum antifungal protein B (PAFB). We report crystal structures of pure PAFB, PAFB in complex with Zn, and the ternary complex of PAFB, Zn and sulfonato-calix[8]arene (sclx). A comparison of the three crystal structures revealed the structural plasticity of PAFB. While the flexible and highly anionic sclx resulted in large molecular weight aggregates of PAFB in solution, diffraction-quality crystals of PAFB-sclx were not obtained. We report crystals of PAFB-Zn-sclx in which a trinuclear zinc cluster occurred adjacent to a calixarene binding site. Interestingly, the combination of sclx complexation and zinc coordination resulted in a porous framework with channels of circa 2 nm diameter. Detailed analysis of the crystal structure highlighted novel molecular recognition features. This research enriches the set of supramolecular interactions available to promote protein assembly.

PubMed: 33631304
DOI: 10.1016/j.jsb.2021.107711

Experimental method

X-RAY DIFFRACTION (1.2 Å)