Document Type
Article
Publication Date
4-23-2013
Abstract
Hemophores from Serratia marcescens (HasAsm) and Pseudomonas aeruginosa (HasAp) bind hemin between two loops, which harbor the axial ligands H32 and Y75. Hemin binding to the Y75 loop triggers closing of the H32 loop and enables binding of H32. Because Yersinia pestis HasA (HasA yp) presents a Gln at position 32, we determined the structures of apo- and holo-HasAyp. Surprisingly, the Q32 loop in apo-HasA yp is already in the closed conformation, but no residue from the Q32 loop binds hemin in holo-HasAyp. In agreement with the minimal reorganization between the apo- and holo-structures, the hemin on-rate is too fast to detect by conventional stopped-flow measurements. © 2013 American Chemical Society.
Publication Source (Journal or Book title)
Biochemistry
First Page
2705
Last Page
2707
Recommended Citation
Kumar, R., Lovell, S., Matsumura, H., Battaile, K., Moënne-Loccoz, P., & Rivera, M. (2013). The hemophore HasA from Yersinia pestis (HasAyp) coordinates hemin with a single residue, Tyr75, and with minimal conformational change. Biochemistry, 52 (16), 2705-2707. https://doi.org/10.1021/bi400280z