Publications
Development and atomic structure of a new fluorescence-based sensor to probe heme transfer in bacterial pathogens. J Inorg Biochem. 249, 112368
(2023) The Shr receptor from uses a cap and release mechanism to acquire heme-iron from human hemoglobin. Proc Natl Acad Sci U S A. 120, e2211939120
(2023) The structure of the Clostridium thermocellum RsgI9 ectodomain provides insight into the mechanism of biomass sensing. Proteins. 10.1002/prot.26326
(2022) Insight into the molecular basis of substrate recognition by the wall teichoic acid glycosyltransferase TagA. J Biol Chem. 10.1016/j.jbc.2021.101464
(2021) (2019) (2019)
The Shr protein captures human hemoglobin using two structurally unique binding domains. J Biol Chem. 293, 18365-18377
(2018) (2016)
Novel mechanism of hemin capture by Hbp2, the hemoglobin-binding hemophore from Listeria monocytogenes. J Biol Chem. 289, 34886-99
(2014) (2014) (2010)