| Structural highlights
9epn is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.7Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
HPRS_ECOLI Member of a two-component regulatory system HprR/HprS involved in response to hydrogen peroxide (PubMed:25568260, PubMed:27983483). Senses H(2)O(2), maybe via the redox state of the membrane (PubMed:27983483). Activates HprR by phosphorylation (PubMed:15522865). Can also phosphorylate CusR (PubMed:15522865).[1] [2] [3]
Publication Abstract from PubMed
The HprSR constitutes the bacterial two-component regulatory system engaged by Escherichia coli to reduce the damaging effects of reactive chlorine and oxygen species present in its cytosol. Hypochlorous acid (HOCl) has been shown to be the molecule capable of activating of the HprSR system. HOCl is produced upon pathogen invasion by phagocytic cells of the human innate immune system, particularly neutrophils, to take advantage of its powerful antimicrobial attributes. Therefore, comprehensive studies concerning bacterial sensing and regulatory HprSR system are indispensable in understanding and effectively eliminating pathogens. Here we present the first crystal structure, solved at 1.7 A resolution, of the HprS cytoplasmic domains arranged as a homodimer. In both protomers, the catalytic ATP-binding domain contains a non-hydrolysable ATP analog coordinated by a magnesium ion. This structure allowed us to provide a detailed characterization of kinase-substrate interaction. Furthermore, the structural data are supported by biophysical studies of kinase interaction with cognate response regulator HprR and substrate ATP. The kinase activity is also assessed in the presence or absence of HprR.
Structural and biophysical characterization of the cytoplasmic domains of HprS kinase and its interactions with the cognate regulator HprR.,Koczurowska A, Carrillo DR, Alai MG, Zaklos-Szyda M, Bujacz G, Pietrzyk-Brzezinska AJ Arch Biochem Biophys. 2025 Feb;764:110269. doi: 10.1016/j.abb.2024.110269. Epub , 2024 Dec 15. PMID:39681306[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yamamoto K, Hirao K, Oshima T, Aiba H, Utsumi R, Ishihama A. Functional characterization in vitro of all two-component signal transduction systems from Escherichia coli. J Biol Chem. 2005 Jan 14;280(2):1448-56. Epub 2004 Nov 2. PMID:15522865 doi:http://dx.doi.org/10.1074/jbc.M410104200
- ↑ Urano H, Umezawa Y, Yamamoto K, Ishihama A, Ogasawara H. Cooperative regulation of the common target genes between H₂O₂-sensing YedVW and Cu²⁺-sensing CusSR in Escherichia coli. Microbiology (Reading). 2015 Apr;161(Pt 4):729-38. PMID:25568260 doi:10.1099/mic.0.000026
- ↑ Urano H, Yoshida M, Ogawa A, Yamamoto K, Ishihama A, Ogasawara H. Cross-regulation between two common ancestral response regulators, HprR and CusR, in Escherichia coli. Microbiology (Reading). 2017 Feb;163(2):243-252. PMID:27983483 doi:10.1099/mic.0.000410
- ↑ Koczurowska A, Carrillo DR, Alai MG, Zakłos-Szyda M, Bujacz G, Pietrzyk-Brzezinska AJ. Structural and biophysical characterization of the cytoplasmic domains of HprS kinase and its interactions with the cognate regulator HprR. Arch Biochem Biophys. 2025 Feb;764:110269. PMID:39681306 doi:10.1016/j.abb.2024.110269
|
