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

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

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...

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Bibliographic Details
Main Authors: Akinobu Senoo, Masato Hoshino, Toshiki Shiomi, Makoto Nakakido, Satoru Nagatoishi, Daisuke Kuroda, Ichiro Nakagawa, Jeremy R. H. Tame, Jose M. M. Caaveiro, Kouhei Tsumoto
Format: Article
Language:English
Published: Nature Portfolio 2024-03-01
Series:Scientific Reports
Subjects:
Hemoglobin
Streptococcus pyogenes
Protein–protein interaction
Heme
Host–pathogen interaction
X-ray crystallography
Online Access:https://doi.org/10.1038/s41598-024-55734-x

Internet

https://doi.org/10.1038/s41598-024-55734-x

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