The protein rTRD is the recombinant form of the target recognition domain of zoocin A, a lytic exoenzyme produced by Streptococcus equi subspecies zooepidemicus 4881. It has no known sequence homologs. However, the catalytic domain of zoocin A is homologous to lysostaphin which is another exoenzyme active against a different spectrum of bacteria, including the pathogen Staphylococcus aureus. An ensemble of models for the solution structure of rTRD has been generated by NMR techniques. The minimum energy model from the ensemble was subjected to three-dimensional homology search engines, but no homologs were found, suggesting rTRD may represent a new protein folding family. There is some similarity in the folding of rTRD to the immunoglobin fold of the antigen binding region of mammalian antibodies which could suggest an ancient evolutionary relation.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1002/prot.24224 | DOI Listing |
Animals (Basel)
June 2020
Department of Animal Science, Life and Industry Convergence Research Institute, Pusan National University, Miryang 50463, Korea.
( ) is one of the critical initiators of acute acidosis in ruminants. Therefore, we aimed to develop and characterize the endolysin LyJH307, which can lyse ruminal . We tested the bactericidal activity of recombinant LyJH307 against S.
View Article and Find Full Text PDFProteins
January 2017
Department of Chemistry, University of Alabama, Tuscaloosa, Alabama, 35487.
Zoocin A is a Zn-metallopeptidase secreted by Streptococcus zooepidemicus strain 4881. Its catalytic domain is responsible for cleaving the D-alanyl-L-alanine peptide bond in streptococcal peptidoglycan. The solution NMR structure of the Cys74 to Ala74 mutant of the recombinant catalytic domain (rCAT C74A) has been determined.
View Article and Find Full Text PDFBiochem Biophys Res Commun
November 2013
Department of Chemistry, University of Alabama, Tuscaloosa, AL 35487, United States.
A docking model is proposed for the target recognition domain of the lytic exoenzyme zoocin A with the peptidoglycan on the outer cell surface of sensitive bacterial strains. Solubilized fragments from such peptidoglycans perturb specific backbone and side chain amide resonances in the recombinant form of the domain designated rTRD as detected in two-dimensional (1)H-(15)N correlation NMR spectra. The affected residues comprise a shallow surface cleft on the protein surface near W115, N53, N117, and Q105 among others, which interacts with the peptide portion of the peptidoglycan.
View Article and Find Full Text PDFProteins
April 2013
Department of Chemistry, University of Alabama, Tuscaloosa, Alabama 35487-0336, USA.
The protein rTRD is the recombinant form of the target recognition domain of zoocin A, a lytic exoenzyme produced by Streptococcus equi subspecies zooepidemicus 4881. It has no known sequence homologs. However, the catalytic domain of zoocin A is homologous to lysostaphin which is another exoenzyme active against a different spectrum of bacteria, including the pathogen Staphylococcus aureus.
View Article and Find Full Text PDFAppl Environ Microbiol
October 2009
Department of Biological Sciences, The University of Alabama, Tuscaloosa, Alabama 35487-0334, USA.
Producer cell immunity to the streptococcolytic enzyme zoocin A, which is a D-alanyl-L-alanine endopeptidase, is due to Zif, the zoocin A immunity factor. Zif has high degrees of similarity to MurM and MurN (members of the FemABX family of proteins), which are responsible for the addition of amino acids to cross bridges during peptidoglycan synthesis in streptococci. In this study, purified peptidoglycans from strains with and without zif were compared to determine how Zif modifies the peptidoglycan layer to cause resistance to zoocin A.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!