2nc2 | pdb_00002nc2

Structure, Dynamics and functional Aspects of the antifungal protein sfPAFB

spinqualitylabelsall models 2nc2, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2nc2 is a 1 chain structure with sequence from Atcc 10106. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: afp, pafB (ATCC 10106) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [AFP_PENCH] Strong antifungal activity against the molds P.commune Pc332, P.echinulatum Pe321, and A.niger An261. Publication Abstract from PubMed Small, cysteine-rich and cationic proteins with antimicrobial activity are produced by diverse organisms of all kingdoms and represent promising molecules for drug development. The ancestor of all industrial penicillin producing strains, the ascomycete Penicillium chryosgenum Q176, secretes the extensively studied antifungal protein PAF. However, the genome of this strain harbours at least two more genes that code for other small, cysteine-rich and cationic proteins with potential antifungal activity. In this study, we characterized the pafB gene product that shows high similarity to PgAFP from P. chrysogenum R42C. Although abundant and timely regulated pafB gene transcripts were detected, we could not identify PAFB in the culture broth of P. chrysogenum Q176. Therefore, we applied a P. chrysogenum-based expression system to produce sufficient amounts of recombinant PAFB to address unanswered questions concerning the structure and antimicrobial function. Nuclear magnetic resonance (NMR)-based analyses revealed a compact beta-folded structure, comprising five beta-strands connected by four solvent exposed and flexible loops and an "abcabc" disulphide bond pattern. We identified PAFB as an inhibitor of growth of human pathogenic moulds and yeasts. Furthermore, we document for the first time an anti-viral activity for two members of the small, cysteine-rich and cationic protein group from ascomycetes. New Antimicrobial Potential and Structural Properties of PAFB: A Cationic, Cysteine-Rich Protein from Penicillium chrysogenum Q176.,Huber A, Hajdu D, Bratschun-Khan D, Gaspari Z, Varbanov M, Philippot S, Fizil A, Czajlik A, Kele Z, Sonderegger C, Galgoczy L, Bodor A, Marx F, Batta G Sci Rep. 2018 Jan 29;8(1):1751. doi: 10.1038/s41598-018-20002-2. PMID:29379111 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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