5ZQD

Crystal Structure of Penicillin-Binding Protein D2 from Listeria monocytogenes in the Cefotaxime bound form

5ZQD の概要

• エントリーDOI: 10.2210/pdb5zqd/pdb
• 分子名称: Lmo2812 protein, CEFOTAXIME, C3' cleaved, open, bound form, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: antibiotics, beta-lactams, dd-carboxypeptidase, lmpbpd2, antibiotic
• 由来する生物種: Listeria monocytogenes EGD-e
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 246515.02

構造登録者

Jeong, J.H.,Kim, Y.G. (登録日: 2018-04-18, 公開日: 2018-07-25, 最終更新日: 2025-09-17)

主引用文献

Jeong, J.H.,Cha, H.J.,Kim, Y.G.
Crystal Structures of Penicillin-Binding Protein D2 from Listeria monocytogenes and Structural Basis for Antibiotic Specificity
Antimicrob. Agents Chemother., 62:-, 2018

PubMed Abstract: β-Lactam antibiotics that inhibit penicillin-binding proteins (PBPs) have been widely used in the treatment of bacterial infections. However, the molecular basis underlying the different inhibitory potencies of β-lactams against specific PBPs is not fully understood. Here, we present the crystal structures of penicillin-binding protein D2 (PBPD2) from , a Gram-positive foodborne bacterial pathogen that causes listeriosis in humans. The acylated structures in complex with four antibiotics (penicillin G, ampicillin, cefotaxime, and cefuroxime) revealed that the β-lactam core structures were recognized by a common set of residues; however, the R1 side chains of each antibiotic participate in different interactions with PBPD2. In addition, the structural complementarities between the side chains of β-lactams and the enzyme were found to be highly correlated with the relative reactivities of penam or cephem antibiotics against PBPD2. Our study provides the structural basis for the inhibition of PBPD2 by clinically important β-lactam antibiotics that are commonly used in listeriosis treatment. Our findings imply that the modification of β-lactam side chains based on structural complementarity could be useful for the development of potent inhibitors against β-lactam-resistant PBPs.

PubMed: 30082290
DOI: 10.1128/AAC.00796-18

実験手法

X-RAY DIFFRACTION (1.888 Å)