Structural highlights
Publication Abstract from PubMed
We have previously isolated the Gram-positive chitin-degrading bacterium Paenibacillus sp. str. FPU-7. This bacterium traps chitin disaccharide (GlcNAc)2 on its cell surface using two homologous solute-binding proteins, NagB1 and NagB2. Bacteria use histidine kinase of the two-component regulatory system as an extracellular environment sensor. In this study, we found that nagS, which encodes a histidine kinase, is located next to the nagB1 gene. Biochemical experiments revealed that the NagS sensor domain (NagS30-294) interacts with the NagB1-(GlcNAc)2 complex. However, proof of NagS30-294 interacting with NagB1 without (GlcNAc)2 is currently unavailable. In contrast to NagB1, no complex formation was observed between NagS30-294 and NagB2, even in the presence of (GlcNAc)2. The NagS30-294 crystal structure at 1.8 A resolution suggested that the canonical tandem-Per-Arnt-Sim (PAS) fold recognizes the NagB1-(GlcNAc)2 complex. This study provides insight into the recognition of chitin oligosaccharides by bacteria.
Characterization of the extracellular domain of sensor histidine kinase NagS from Paenibacillus sp. str. FPU-7: nagS interacts with oligosaccharide binding protein NagB1 in complexes with N, N'-diacetylchitobiose.,Itoh T, Ogawa T, Hibi T, Kimoto H Biosci Biotechnol Biochem. 2023 Dec 6:zbad173. doi: 10.1093/bbb/zbad173. PMID:38059852[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Itoh T, Ogawa T, Hibi T, Kimoto H. Characterization of the extracellular domain of sensor histidine kinase NagS from Paenibacillus sp. str. FPU-7: nagS interacts with oligosaccharide binding protein NagB1 in complexes with N, N'-diacetylchitobiose. Biosci Biotechnol Biochem. 2023 Dec 6:zbad173. PMID:38059852 doi:10.1093/bbb/zbad173
