scholarly journals Regulation of the Bacterial Cell Wall: Analysis of a Mutant of Bacillus subtilis Defective in Biosynthesis of Teichoic Acid

1972 ◽  
Vol 110 (1) ◽  
pp. 281-290 ◽  
Author(s):  
R. J. Boylan ◽  
N. H. Mendelson ◽  
D. Brooks ◽  
F. E. Young
1973 ◽  
Vol 37 (2) ◽  
pp. 389-400 ◽  
Author(s):  
Mireille Leduc ◽  
Jean Heijenoort ◽  
Marie Kaminski ◽  
Jekisiel Szulmajster

Science ◽  
2013 ◽  
Vol 341 (6149) ◽  
pp. 1012-1016 ◽  
Author(s):  
Ben C. Chung ◽  
Jinshi Zhao ◽  
Robert A. Gillespie ◽  
Do-Yeon Kwon ◽  
Ziqiang Guan ◽  
...  

MraY (phospho-MurNAc-pentapeptide translocase) is an integral membrane enzyme that catalyzes an essential step of bacterial cell wall biosynthesis: the transfer of the peptidoglycan precursor phospho-MurNAc-pentapeptide to the lipid carrier undecaprenyl phosphate. MraY has long been considered a promising target for the development of antibiotics, but the lack of a structure has hindered mechanistic understanding of this critical enzyme and the enzyme superfamily in general. The superfamily includes enzymes involved in bacterial lipopolysaccharide/teichoic acid formation and eukaryotic N-linked glycosylation, modifications that are central in many biological processes. We present the crystal structure of MraY from Aquifex aeolicus (MraYAA) at 3.3 Å resolution, which allows us to visualize the overall architecture, locate Mg2+ within the active site, and provide a structural basis of catalysis for this class of enzyme.


2009 ◽  
Vol 16 (5) ◽  
pp. 548-556 ◽  
Author(s):  
Michael A. D'Elia ◽  
Kathryn E. Millar ◽  
Amit P. Bhavsar ◽  
Ana M. Tomljenovic ◽  
Bernd Hutter ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document