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Protein & Peptide Letters


ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Structural Bioinformatics of Vibrio cholerae Aminopeptidase A (PepA) Monomer

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

Volume 16, Issue 1, 2009

Page: [36 - 45] Pages: 10

DOI: 10.2174/092986609787049484

Price: $65


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.

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

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