1B2V

HEME-BINDING PROTEIN A

Summary for 1B2V

• Entry DOI: 10.2210/pdb1b2v/pdb
• Descriptor: PROTEIN (HEME-BINDING PROTEIN A), CALCIUM ION, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• Functional Keywords: heme acquisition, iron metabolism, transport protein
• Biological source: Serratia marcescens
• Cellular location: Secreted : Q54450
• Total number of polymer chains: 1
• Total formula weight: 19945.20

Authors

Arnoux, P.,Haser, R.,Izadi, N.,Lecroisey, A.,Wandersma, N.C.,Czjzek, M. (deposition date: 1998-12-01, release date: 1999-06-24, Last modification date: 2023-12-27)

Primary citation

Arnoux, P.,Haser, R.,Izadi, N.,Lecroisey, A.,Delepierre, M.,Wandersman, C.,Czjzek, M.
The crystal structure of HasA, a hemophore secreted by Serratia marcescens.
Nat.Struct.Biol., 6:516-520, 1999

PubMed Abstract: Free iron availability is strongly limited in vertebrate hosts, making the iron acquisition by siderophores inappropriate. Pathogenic bacteria have developed various ways to use the host's iron from iron-containing proteins. Serratia marcescens can use the iron from hemoglobin through the secretion of a hemophore called HasA, which takes up the heme from hemoglobin and shuttles it to the receptor HasR, which in turn, releases heme into the bacterium. We report here the first crystal structure of such a hemophore, bound to a heme group at two different pH values and at a resolution of 1.9 A. The structure reveals a new original fold and suggests a hypothetical mechanism for both heme uptake and release.

PubMed: 10360351
DOI: 10.1038/9281

Experimental method

X-RAY DIFFRACTION (1.9 Å)