Structural Bioinformatics of Vibrio cholerae Aminopeptidase A (PepA) Monomer

Title: Structural Bioinformatics of Vibrio cholerae Aminopeptidase A (PepA) Monomer

Volume: 16 Issue: 1

Author(s): Ghosia Lutfullah, Noreen Azhar, Farhat Amin, Zahid Khan, M. Kamran Azim, Khalida Shouqat, Sajid Noor and Rizwan Ali

Affiliation:

Keywords: Aminopeptidase (PepA) Vibrio cholerae, protein degradation, homohexamer, homology modeling, 3D structure, DNA binding

Abstract: Aminopeptidase A (PepA) is a metalloexopeptidase found in Vibrio cholerae .It functions as a transcriptional repressor in regulatory cascade that controls virulence gene expression in V. cholerae. It is involved in protein degradation and in the metabolism of biologically active peptides. We proposed a 3D model of PepA based upon the crystal structure of PepA from Escherichia coli (E. coli) with an intention to evaluate the active site of the enzyme and to predict the properties of this enzyme, study of its 3D structure will help in understanding its role in DNA binding.

Cite this article as:

Lutfullah Ghosia, Azhar Noreen, Amin Farhat, Khan Zahid, Azim Kamran M., Shouqat Khalida, Noor Sajid and Ali Rizwan, Structural Bioinformatics of Vibrio cholerae Aminopeptidase A (PepA) Monomer, Protein & Peptide Letters 2009; 16 (1) . https://dx.doi.org/10.2174/092986609787049484