دورية أكاديمية

Structural Insights into the Penicillin-Binding Protein 4 (DacB) from Mycobacterium tuberculosis

التفاصيل البيبلوغرافية
العنوان: Structural Insights into the Penicillin-Binding Protein 4 (DacB) from Mycobacterium tuberculosis
المؤلفون: Sung-Min Kang, Do-Hee Kim
المصدر: International Journal of Molecular Sciences, Vol 25, Iss 2, p 983 (2024)
بيانات النشر: MDPI AG, 2024.
سنة النشر: 2024
المجموعة: LCC:Biology (General)
LCC:Chemistry
مصطلحات موضوعية: Mycobacterium tuberculosis, antibiotics, penicillin-binding protein, Biology (General), QH301-705.5, Chemistry, QD1-999
الوصف: Mycobacterium tuberculosis, a major cause of mortality from a single infectious agent, possesses a remarkable mycobacterial cell envelope. Penicillin-Binding Proteins (PBPs) are a family of bacterial enzymes involved in the biosynthesis of peptidoglycan. PBP4 (DacB) from M. tuberculosis (MtbPBP4) has been known to function as a carboxypeptidase, and the role and significance of carboxypeptidases as targets for anti-tuberculosis drugs or antibiotics have been extensively investigated over the past decade. However, their precise involvement remains incompletely understood. In this study, we employed predictive modeling and analyzed the three-dimensional structure of MtbPBP4. Interestingly, MtbPBP4 displayed a distinct domain structure compared to its homologs. Docking studies with meropenem verified the presence of active site residues conserved in PBPs. These findings establish a structural foundation for comprehending the molecular function of MtbPBP4 and offer a platform for the exploration of novel antibiotics.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1422-0067
1661-6596
Relation: https://www.mdpi.com/1422-0067/25/2/983; https://doaj.org/toc/1661-6596; https://doaj.org/toc/1422-0067
DOI: 10.3390/ijms25020983
URL الوصول: https://doaj.org/article/0e5f39d36bc94bd7b4aea645775de01d
رقم الأكسشن: edsdoj.0e5f39d36bc94bd7b4aea645775de01d
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:14220067
16616596
DOI:10.3390/ijms25020983