1b2v | pdb_00001b2v
HEME-BINDING PROTEIN A
Structural highlights
Function[HASA_SERMA] Can bind free heme and also acquire it from hemoglobin. Conveys heme from hemoglobin to the HasR receptor which releases it into the bacterium. HasR alone can take up heme but the synergy between HasA and HasR increases heme uptake 100-fold.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedFree 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. The crystal structure of HasA, a hemophore secreted by Serratia marcescens.,Arnoux P, Haser R, Izadi N, Lecroisey A, Delepierre M, Wandersman C, Czjzek M Nat Struct Biol. 1999 Jun;6(6):516-20. PMID:10360351[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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