Premium
Cover Feature: Structural Mapping of Anion Inhibitors to β‐Carbonic Anhydrase psCA3 from Pseudomonas aeruginosa (ChemMedChem 19/2018)
Author(s) -
Murray Akilah B.,
Aggarwal Mayank,
Pinard Melissa,
Vullo Daniela,
Patrauchan Marianna,
Supuran Claudiu T.,
McKenna Robert
Publication year - 2018
Publication title -
chemmedchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201800628
Subject(s) - pseudomonas aeruginosa , carbonic anhydrase , chemistry , microbiology and biotechnology , cystic fibrosis , bacteria , biochemistry , enzyme , biology , genetics
The Cover Feature illustrates the crystal structure of dimeric β‐carbonic anhydrase, psCA3, found in Pseudomonas aeruginosa . This multidrug‐resistant bacterium commonly causes life‐threatening nosocomial infections and is a key bacterial agent in cystic fibrosis patients. Therefore, discovering novel drug targets against this bacterium is critical. As carbonic anhydrases are necessary for growth and function of Pseudomonas aeruginosa , they can be targeted for antibiotic development. This work shows the first inhibitor structures bound to psCA3 and is fundamental in establishing structure‐based drug design against Pseudomonas aeruginosa . More information can be found in the Full Paper by Robert McKenna et al. on page 2024 in Issue 19, 2018 (DOI: 10.1002/cmdc.201800375).