Solution structure of the Cys74 to Ala74 mutant of the recombinant catalytic domain of Zoocin A

2016 ◽  
Vol 85 (1) ◽  
pp. 177-181 ◽  
Author(s):  
Minli Xing ◽  
Robin S. Simmonds ◽  
Russell Timkovich
Keyword(s):  
Solution Structure ◽  
Catalytic Domain ◽  
Zoocin A

scholarly journals Solution structure of the catalytic domain of human stromelysin complexed with a hydrophobic inhibitor

1995 ◽  
Vol 4 (12) ◽  
pp. 2487-2498 ◽  
Author(s):  
Steven R. Van Doren ◽  
Alexander V. Kurochkin ◽  
Weidong Hu ◽  
Qi-Zhuang Ye ◽  
Linda L. Johnson ◽  
...  
Keyword(s):  
Solution Structure ◽  
Catalytic Domain

scholarly journals Solution structure of the N-terminal catalytic domain of human H-REV107 - A novel circular permutated NlpC/P60 domain

FEBS Letters ◽  
2010 ◽  
Vol 584 (19) ◽  
pp. 4222-4226 ◽  
Author(s):  
Xiaobai Ren ◽  
Jian Lin ◽  
Changwen Jin ◽  
Bin Xia
Keyword(s):  
Solution Structure ◽  
Catalytic Domain

Solution structure of the catalytic domain of γδ resolvase. Implications for the mechanism of catalysis 1 1Edited by P. E. Wright

2001 ◽  
Vol 310 (5) ◽  
pp. 1089-1107 ◽  
Author(s):  
Borlan Pan ◽  
Mark W Maciejewski ◽  
Assen Marintchev ◽  
Gregory P Mullen
Keyword(s):  
Solution Structure ◽  
Catalytic Domain ◽  
Mechanism Of Catalysis

Solution structure of the catalytic domain of RICH protein from goldfish

FEBS Journal ◽  
2007 ◽  
Vol 274 (6) ◽  
pp. 1600-1609 ◽  
Author(s):  
Guennadi Kozlov ◽  
Alexey Y. Denisov ◽  
Ekaterina Pomerantseva ◽  
Michel Gravel ◽  
Peter E. Braun ◽  
...  
Keyword(s):  
Solution Structure ◽  
Catalytic Domain

Solution Structure of the Catalytic Domain of Human Stromelysin-1 Complexed to a Potent, Nonpeptidic Inhibitor

Biochemistry ◽  
1998 ◽  
Vol 37 (40) ◽  
pp. 14048-14056 ◽  
Author(s):  
Yu-Chin Li ◽  
Xiaolu Zhang ◽  
Richard Melton ◽  
Vishwas Ganu ◽  
Nina C. Gonnella
Keyword(s):  
Solution Structure ◽  
Catalytic Domain

Solution structure and DNA binding of the catalytic domain of the large serine resolvase TnpX

2015 ◽  
Vol 28 (5) ◽  
pp. 316-324 ◽  
Author(s):  
Stephen J. Headey ◽  
Andrew Sivakumaran ◽  
Vicki Adams ◽  
Dena Lyras ◽  
Julian I. Rood ◽  
...  
Keyword(s):  
Dna Binding ◽  
Solution Structure ◽  
Catalytic Domain

scholarly journals Solution Structure of the MAPK Phosphatase PAC-1 Catalytic Domain

Structure ◽  
2003 ◽  
Vol 11 (2) ◽  
pp. 155-164 ◽  
Author(s):  
Amjad Farooq ◽  
Olga Plotnikova ◽  
Gaurav Chaturvedi ◽  
Sherry Yan ◽  
Lei Zeng ◽  
...  
Keyword(s):  
Solution Structure ◽  
Catalytic Domain ◽  
Mapk Phosphatase

scholarly journals Zif, the Zoocin A Immunity Factor, Is a FemABX-Like Immunity Protein with a Novel Mode of Action

2009 ◽  
Vol 75 (19) ◽  
pp. 6205-6210 ◽  
Author(s):  
Shaw R. Gargis ◽  
Amy S. Gargis ◽  
Harry E. Heath ◽  
Lucie S. Heath ◽  
Paul A. LeBlanc ◽  
...  
Keyword(s):  
Catalytic Domain ◽  
Negative Ion ◽  
Peptidoglycan Synthesis ◽  
Cell Immunity ◽  
Zoocin A ◽  
Immunity Factor ◽  
Producer Cell ◽  
Cross Bridges ◽  
Negative Ion Mode ◽  
Phage Lysin

ABSTRACT 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. The peptidoglycan from each strain was hydrolyzed using the streptococcolytic phage lysin B30, and the resulting muropeptides were separated by reverse-phase high-pressure liquid chromatography, labeled with 4-sulfophenyl isothiocyanate, and analyzed by tandem mass spectrometry in the negative-ion mode. It was determined that Zif alters the peptidoglycan by increasing the proportion of cross bridges containing three l-alanines instead of two. This modification decreased binding of the recombinant target recognition domain of zoocin A to peptidoglycan. Zif-modified peptidoglycan also was less susceptible to hydrolysis by the recombinant catalytic domain of zoocin A. Thus, Zif is a novel FemABX-like immunity factor because it provides resistance to a bacteriolytic endopeptidase by lengthening the peptidoglycan cross bridge rather than by causing an amino acid substitution.

Solution structure of the recombinant target recognition domain of zoocin A

2013 ◽  
Vol 81 (4) ◽  
pp. 722-727 ◽  
Author(s):  
Yinghua Chen ◽  
Robin S. Simmonds ◽  
John K. Young ◽  
Russell Timkovich
Keyword(s):  
Solution Structure ◽  
Target Recognition ◽  
Zoocin A
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