Structure modeling of a metalloendopeptidase from Corynebacterium pseudotuberculosis.

Abstract

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.

• Authors: 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
• Journal: Computers in biology and medicine (Comput Biol Med) Vol. 42 Issue 5 Pg. 538-41 (May 2012) ISSN: 1879-0534 [Electronic] United States
• PMID: 22342425 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: Copyright © 2012 Elsevier Ltd. All rights reserved.

Chemical References

• Metalloendopeptidases

Topics

• Amino Acid Sequence
• Corynebacterium pseudotuberculosis (enzymology)
• Metalloendopeptidases (chemistry, isolation & purification)
• Models, Molecular
• Molecular Dynamics Simulation
• Molecular Sequence Data
• Protein Conformation
• Sequence Homology, Amino Acid