An in silico approach for structural and functional analysis of heavy metal associated (HMA) proteins in Brassica oleracea

Jasmin Sutkovic, Mujo Kekić, Maida Ljubijankić, Petar Glamočlija

Abstract


Heavy metal ATPases (HMAs) are the most important proteins involved in heavy metal accumulation process. Brassica oleracea has 5 HMA (1-5) homologues whose 3D structure has been predicted and validated in this study by different bioinformatics tools. Phylogenetic and multiple sequence alignment analyses showed high relationship between HMA2 and HMA4, while two same domains were identified in all five HMA proteins: E1-E2 ATPase and haloacid dehydrogenase (HAD) domain. Four HMA (2-5) proteins were identified to be localized in the plasma membrane, while HMA1 localization is predicted to be in plastid. Interactome analysis revealed high interaction of all HMA (1-5) proteins with many metal ion binding proteins and chaperones. Among these, interesting and strong interaction is observed between all HMA (1-5) proteins and ATX1, while HMA1, HMA2 and HMA4 have been found to strongly interact with FP3 (farnesylated protein 3) and FP6 (farnesylated protein 6) proteins. Docking site predictions and electrostatic potentials between HMA2/HMA4 and the interactome proteins were explained and discussed in this study.

Keywords


Keywords: Protein structure prediction, Heavy metals; accumulation; transport; interactome; docking site

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DOI: http://dx.doi.org/10.21533/pen.v4i2.63

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ISSN: 2303-4521

Digital Object Identifier DOI: 10.21533/pen

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This work is licensed under a Creative Commons Attribution 4.0 International License