1b2v | pdb_00001b2v

HEME-BINDING PROTEIN A

spinqualitylabelsall models 1b2v, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1b2v is a 1 chain structure with sequence from Serratia marcescens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: CA, HEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. 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 PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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