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Crystal structure of the sensor domain of the transcriptional regulator HcpR from Porphyromonas GingivalisCrystal structure of the sensor domain of the transcriptional regulator HcpR from Porphyromonas Gingivalis
Structural highlights
Publication Abstract from PubMedAlthough the HcpR regulator plays a vital step in initiation of the nitrosative stress response in many Gram-negative anaerobic bacteria, the molecular mechanisms that it uses to mediate gas sensing are not well understood. Here, a 2.6 A resolution crystal structure of the N-terminal sensing domain of the anaerobic periodontopathogen Porphyromonas gingivalis HcpR is presented. The protein has classical features of the regulators belonging to the FNR-CRP family and contains a hydrophobic pocket in its N-terminal sensing domain. It is shown that heme bound to HcpR exhibits heme iron as a hexacoordinate system in the absence of nitric oxide (NO) and that upon nitrosylation it transitions to a pentacoordinate system. Finally, small-angle X-ray scattering experiments on full-length HcpR reveal that the C-terminal DNA-binding domain of HcpR has a high degree of interdomain flexibility. Nitrosative stress sensing in Porphyromonas gingivalis: structure of and heme binding by the transcriptional regulator HcpR.,Belvin BR, Musayev FN, Burgner J, Scarsdale JN, Escalante CR, Lewis JP Acta Crystallogr D Struct Biol. 2019 Apr 1;75(Pt 4):437-450. doi:, 10.1107/S205979831900264X. Epub 2019 Apr 5. PMID:30988260[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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