Premium
R61 D,D‐peptidase bound to a Helen‐1 Penicillin Substrate or One “Hel”‐en of an Antibiotic
Author(s) -
SosaGonzalez Sonia,
Cobb Michaun,
Osadame Ngozi,
Osademe Isioma,
Campbell Kyler,
Marin Merari,
Llamosa Jhordy Rios,
Llamosa Brigitte Rios,
Jones Kasaundra,
Garland Meg,
Johnson Carol,
Silvaggi Nicholas
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.lb232
Subject(s) - peptidoglycan , antibiotics , penicillin , penicillin binding proteins , bacterial cell structure , bacteria , cell wall , enzyme , microbiology and biotechnology , antibiotic resistance , biochemistry , active site , chemistry , biology , genetics
Although antibiotics like penicillin save lives, antibiotic‐resistant bacteria are a growing issue. According to Purdom (2007), over 70% of infections acquired by hospital patients post‐admission, are resistant to at least one prescribed antibiotic. Penicillin, a β‐lactam antibiotic, treats bacterial infections caused by bacteria producing toxins within a host. Many pathogenic bacteria need a peptidoglycan cell wall for normal functionality. Enzymes in the cell membrane help form this cell wall by cross‐linking peptidoglycan units. β‐lactam antibiotics hinder bacterial cell wall biosynthesis by competing with the peptide substrate for the active site in these enzymes. While not the main enzyme used to produce bacterial cell walls, R61 DD‐peptidase, a cytoplasmic enzyme, is easily crystallized to show bacterial enzyme chemistry. The active site of R61 consists of amino acid residues Ser62, Lys65, Lys159, Arg285, Thr299, and Thr301. The Messmer SMART Team modeled R61 complexed with Helen‐1, a species‐specific β‐lactam, highlighting the functionality and chemistry of the active site amino acids and their interaction with the beta‐lactam. Understanding the structure and function of the active site of penicillin binding proteins, like R61, could lead to new, species‐specific antibiotics that could prevent antibiotic resistance in bacteria. Supported by a grant from NIH‐CTSA UL1RR031973.