HOMOLOGY MODELING AND STRUCTURAL STUDIES OF POTENTIALLY SECRETED CELL WALL PROTEIN ZN-CU SOD FROM NEUROSPORA CRASSA
S. K. Gousia, T. V. Padmavathi, N. V. Ramana and J. Naveena Lavanya Latha*
Background: The cell wall may work as an obstacle by keeping proteins from spilling into the medium and go about as a system for revealing cell wall proteins (CWPs) to the cell surface. Metal particles, for example, copper, iron, and zinc and others assume a crucial part in living life forms fundamentally by virtue of their relationship with proteins, which are referred to as metalloproteins. Copper essentiality holds both its action in structural stabilization and its redox capacity, which is utilized by metalloenzymes that catalyze electron exchange responses. The most advanced utilitarian classifications in the Zn proteome were those identified with transcription, cell cycle, and DNA processing, and in addition protein in fate and modification. Methods: The stereo chemical quality of the protein model was checked by using insilico analysis with PROCHECK and QMEAN servers. The metal binding sites were determined by CHED. Results: In the present study, the authors found that the protein under study contained 7 metal binding sites shows highest metal binding probability for the metal namely calcium in sites 2, 3, 4 & 7 with the metal probability of 0.691595, 0.627722, 0.398702 & 0.304824; Copper in sites 1&5 with the probability of 0.407987 & 0.520100 and zinc in sites 1, 4, 6 & 7 with the probability of 0.473539, 0.411537, 0.595477 & 0.527491 were showed. Conclusions: The result of the study may be a guiding point for further investigations on Zn-Cu SOD protein and metal binding sites. Significant Statement: The Zn-Cu SOD protein extracted from cells of N.crassa was found to possess 7 metal binding sites of which four were found to have high probability towards calcium, two for copper and four sites for zinc.
Keywords: Zn-Cu SOD, Cell binding protein, Neurospora crassa, homology modeling, metal binding sites.
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