Structural basis for the recognition of human hemoglobin by the heme-acquisition protein Shr from Streptococcus pyogenes

Autor:	Akinobu Senoo, Masato Hoshino, Toshiki Shiomi, Makoto Nakakido, Satoru Nagatoishi, Daisuke Kuroda, Ichiro Nakagawa, Jeremy R. H. Tame, Jose M. M. Caaveiro, Kouhei Tsumoto
Jazyk:	angličtina
Rok vydání:	2024
Předmět:	Hemoglobin Streptococcus pyogenes Protein–protein interaction Heme Host–pathogen interaction X-ray crystallography Medicine Science
Zdroj:	Scientific Reports, Vol 14, Iss 1, Pp 1-10 (2024)
Druh dokumentu:	article
ISSN:	2045-2322
DOI:	10.1038/s41598-024-55734-x
Popis:	Abstract In Gram-positive bacteria, sophisticated machineries to acquire the heme group of hemoglobin (Hb) have evolved to extract the precious iron atom contained in it. In the human pathogen Streptococcus pyogenes, the Shr protein is a key component of this machinery. Herein we present the crystal structure of hemoglobin-interacting domain 2 (HID2) of Shr bound to Hb. HID2 interacts with both, the protein and heme portions of Hb, explaining the specificity of HID2 for the heme-bound form of Hb, but not its heme-depleted form. Further mutational analysis shows little tolerance of HID2 to interfacial mutations, suggesting that its interaction surface with Hb could be a suitable candidate to develop efficient inhibitors abrogating the binding of Shr to Hb.
Databáze:	Directory of Open Access Journals
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