5v30

Publication Abstract from PubMed

Although 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.