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Publication Abstract from PubMed

Bacterial sugar kinase is a central enzyme for proper sugar degradation in bacteria, essential for survival and growth. Therefore, this enzyme family is a primary target for antibacterial drug development, with YdjH most preferring to phosphorylate higher-order monosaccharides with a carboxylate terminus. Sugar kinases express diverse specificity and functions, making specificity determination of this family a prominent issue. This study examines the YdjH crystal structure from Acinetobacter baumannii (abYdjH), which has an exceptionally high antibiotic resistance and is considered a superbug. Our structural and biochemical study revealed that abYdjH has a widely open lid domain and is a solution dimer. In addition, the putative active site of abYdjH was determined based on structural analysis, sequence comparison, and in silico docking. Finally, we proposed the active site-forming residues that determine various sugar specificities from abYdjH. This study contributes towards a deeper understanding of the phosphorylation process and bacterial sugar metabolism of YdjH family to design the next-generation antibiotics for targeting A. baumannii.

Structure of YdjH from Acinetobacter baumannii revealed an active site of YdjH family sugar kinase.,Lee GH, Kim JH, Ha HJ, Park HH Biochem Biophys Res Commun. 2023 Apr 22;664:27-34. doi: , 10.1016/j.bbrc.2023.04.073. PMID:37130458^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.