In-silico structural modelling of cytochrome complex proteins of white turmeric (Curcuma zedoaria (Christm.) Roscoe

Abstract

Curcuma zedoaria (Christm.) Roscoe (white turmeric) is a perennial herba-ceous plant of family Zingiberaceae and mainly found in the wild areas of tropical and subtropical regions worldwide. The cytochrome proteins in plants play important roles in promoting their growth and development, as well as protecting them from stresses and diseases. Cytochrome proteins like psbF, psbE, petB, petD, petN, petG and ccsA play important roles in deg-radation of misfolded proteins, ATP formation, cyclic electron flow and bio-genesis of c-type cytochrome of C. zedoaria. However, due to lack of struc-tural availability of these C. zedoaria cytochrome proteins in structural data-bases, the physiochemical parameters of sequences were estimated using Expasy ProtParam web tool. Self-Optimized Prediction Method with Align-ment (SOPMA) server and MODELLER version 9.23 were used for modelling along with Qualitative Model Energy Analysis (QMEAN) and Protein Struc-ture Analysis (ProSA) servers were implemented for validating the second-ary and tertiary structures of these proteins. The obtained QMEAN4 values of the modelled cytochrome proteins were -2.04, -1.20, -3.01, -1.57, -2.11, - 1.74 and -12.87. The Z-scores obtained from ProSA server were 0.5, -0.83, - 1.5, -0.58, -0.02, 0.14 and -3.73. All seven modelled structures have been submitted to protein model database (PMDB). The derived results will be helpful in further investigations towards determining the crystal structure of the hypothetical proteins, structural motifs, physiochemical properties and also protein-protein interaction studies of various cytochrome proteins.