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.
References
Mar 5, 1992·Nature·R LüthyD Eisenberg
Jul 12, 1991·Science·J U BowieD Eisenberg
Apr 15, 1991·The Biochemical Journal·N D Rawlings, A J Barrett
Jan 2, 1989·FEBS Letters·C V JongeneelA Bairoch
Dec 1, 1993·Proteins·M J Sippl
May 22, 1998·Journal of Molecular Biology·F Melo, E Feytmans
Aug 15, 2000·Annual Review of Biophysics and Biomolecular Structure·M A Martí-RenomA Sali
Jun 23, 2001·Protein Science : a Publication of the Protein Society·O Carugo, S Pongor
Dec 6, 2003·Structure·Jingzhi LiBingdong Sha
Dec 23, 2003·Journal of Molecular Biology·Sergey G OdintsovMatthias Bochtler
Dec 24, 2003·Protein Science : a Publication of the Protein Society·Hao Fan, Alan E Mark
Oct 15, 2005·Australian and New Zealand Journal of Public Health·Andrew C HuiMichael B Barton
Feb 14, 2006·Veterinary Research·Fernanda Alves DorellaVasco Azevedo
May 23, 2007·Nucleic Acids Research·Markus Wiederstein, Manfred J Sippl
May 24, 2008·Proteins·Delphine C BasJan H Jensen
Jul 12, 1972·Nature: New Biology·K TitaniH Neurath
Feb 2, 2010·Journal of Inorganic Biochemistry·Xue LiKenneth M Merz
May 3, 2011·PloS One·Jerônimo C RuizVasco Azevedo