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细菌药物靶点的结构基因组学:应用高通量流程解析58种致病及相关细菌的蛋白质结构

Structural genomics of bacterial drug targets: Application of a high-throughput pipeline to solve 58 protein structures from pathogenic and related bacteria.

作者信息

Inniss Nicole L, Minasov George, Chang Changsoo, Tan Kemin, Kim Youngchang, Maltseva Natalia, Stogios Peter, Filippova Ekaterina, Michalska Karolina, Osipiuk Jerzy, Jaroszewki Lukasz, Godzik Adam, Savchenko Alexei, Joachimiak Andrzej, Anderson Wayne F, Satchell Karla J F

机构信息

Department of Microbiology-Immunology, Northwestern University, Feinberg School of Medicine, Chicago, Illinois, USA.

Center for Structural Biology of Infectious Diseases, Feinberg School of Medicine, Northwestern University, Chicago, Illinois, USA.

出版信息

Microbiol Resour Announc. 2025 Jun 12;14(6):e0020025. doi: 10.1128/mra.00200-25. Epub 2025 May 20.

DOI:10.1128/mra.00200-25
PMID:40391899
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC12160482/
Abstract

Antibiotic resistance remains a leading cause of severe infections worldwide. Small changes in protein sequence can impact antibiotic efficacy. Here, we report deposition of 58 X-ray crystal structures of bacterial proteins that are known targets for antibiotics, which expands knowledge of structural variation to support future antibiotic discovery or modifications.

摘要

抗生素耐药性仍然是全球严重感染的主要原因。蛋白质序列的微小变化会影响抗生素疗效。在此,我们报告了58种细菌蛋白质的X射线晶体结构的存贮情况,这些蛋白质是已知的抗生素作用靶点,这拓展了结构变异方面的知识,以支持未来的抗生素发现或改良。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/16b5/12160482/311d2b1f3a60/mra.00200-25.f001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/16b5/12160482/311d2b1f3a60/mra.00200-25.f001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/16b5/12160482/311d2b1f3a60/mra.00200-25.f001.jpg

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Structural comparison of p-hydroxybenzoate hydroxylase (PobA) from Pseudomonas putida with PobA from other Pseudomonas spp. and other monooxygenases.恶臭假单胞菌对羟基苯甲酸羟化酶(PobA)与其他假单胞菌属的PobA及其他单加氧酶的结构比较。
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