1dk0

CRYSTAL STRUCTURE OF THE HEMOPHORE HASA FROM SERRATIA MARCESCENS CRYSTAL FORM P2(1), PH8

spinqualitylabelsall models 1dk0, resolution 1.77Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1dk0 is a 2 chain structure with sequence from "bacillus_marcescens"_(bizio_1823)_trevisan_in_de_toni_and_trevisan_1889 "bacillus marcescens" (bizio 1823) trevisan in de toni and trevisan 1889. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HEM Related: 1b2v, 1dkh 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 The protein HasA from the Gram negative bacteria Serratia marcescens is the first hemophore to be described at the molecular level. It participates to the shuttling of heme from hemoglobin to the outer membrane receptor HasR, which in turn releases it into the bacterium. HasR alone is also able to take up heme from hemoglobin but synergy with HasA increases the efficiency of the system by a factor of about 100. This iron acquisition system allows the bacteria to survive with hemoglobin as the sole iron source. Here we report the structures of a new crystal form of HasA diffracting up to 1.77A resolution as well as the refined structure of the trigonal crystal form diffracting to 3.2A resolution. The crystal structure of HasA at high resolution shows two possible orientations of the heme within the heme-binding pocket, which probably are functionally involved in the heme-iron acquisition process. The detailed analysis of the three known structures reveals the molecular basis regulating the relative affinity of the heme/hemophore complex. Functional aspects of the heme bound hemophore HasA by structural analysis of various crystal forms.,Arnoux P, Haser R, Izadi-Pruneyre N, Lecroisey A, Czjzek M Proteins. 2000 Nov 1;41(2):202-10. PMID:10966573 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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