Structure modeling of a metalloendopeptidase from Corynebacterium pseudotuberculosis.

Luis C Guimarães, Natália F Silva, Anderson Miyoshi, Maria P C Schneider, Artur Silva, Vasco Azevedo, Davi S B Brasil, Jerônimo Lameira, Cláudio N Alves

Laboratório de Polimorfismo de DNA, Instituto de Ciências Biológicas, Universidade Federal do Pará, Belém, PA, Brazil.

Computers in biology and medicine 2012 May

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Metalloendopeptidases are zinc-dependent hydrolases enzymes with many different roles in biological systems, ranging from remodeling conjunctive tissue to removing signaling sequences from nascent proteins. Here, we describe the three-dimensional structure of the metalloendopeptidase from Corynebacterium pseudotuberculosis generated by homology modeling and molecular dynamics. Analysis of key distances shows that His-132, Asp-136, His-211, Leu-212 and one molecule of water play an important role in the protein-Zn(2+) ion interaction. The model obtained may provide structural insights into this enzyme and can be useful for the design of new caseous lymphadenitis vaccines based on genetic attenuation from key point mutation. Copyright © 2012 Elsevier Ltd. All rights reserved.

Citation

Luis C Guimarães, Natália F Silva, Anderson Miyoshi, Maria P C Schneider, Artur Silva, Vasco Azevedo, Davi S B Brasil, Jerônimo Lameira, Cláudio N Alves. Structure modeling of a metalloendopeptidase from Corynebacterium pseudotuberculosis. Computers in biology and medicine. 2012 May;42(5):538-41