8W7P

Extracellular domain of a sensor histidine kinase

Summary for 8W7P

• Entry DOI: 10.2210/pdb8w7p/pdb
• Descriptor: Extracellular domain of a sensor histidine kinase NagS, GLYCEROL (3 entities in total)
• Functional Keywords: sensor histidine kinase, signaling protein
• Biological source: Paenibacillus sp. FPU-7
• Total number of polymer chains: 2
• Total formula weight: 64184.04

Authors

Itoh, T.,Ogawa, T.,Hibi, T.,Kimoto, H. (deposition date: 2023-08-31, release date: 2024-01-10, Last modification date: 2024-03-06)

Primary citation

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., 88:294-304, 2024

PubMed Abstract: 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 (HK) of the two-component regulatory system as an extracellular environment sensor. In this study, we found that nagS, which encodes a HK, 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 Å resolution suggested that the canonical tandem-Per-Arnt-Sim fold recognizes the NagB1-(GlcNAc)2 complex. This study provides insight into the recognition of chitin oligosaccharides by bacteria.

PubMed: 38059852
DOI: 10.1093/bbb/zbad173

Experimental method

X-RAY DIFFRACTION (1.8 Å)