7re4 | pdb_00007re4

Apo Hemophilin from A. baumannii

spinqualitylabelsall models 7re4, resolution 1.87Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7re4 is a 3 chain structure with sequence from Acinetobacter baumannii NIPH 201. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.87Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A086I049_ACIBA Publication Abstract from PubMed Nutrient acquisition systems are often crucial for pathogen growth and survival during infection, and represent attractive therapeutic targets. Here, we study the protein machinery required for heme uptake in the opportunistic pathogen Acinetobacter baumannii. We show that the hemO locus, which includes a gene encoding the heme-degrading enzyme, is required for high-affinity heme acquisition from hemoglobin and serum albumin. The hemO locus includes a gene coding for a heme scavenger (HphA), which is secreted by a Slam protein. Furthermore, heme uptake is dependent on a TonB-dependent receptor (HphR), which is important for survival and/or dissemination into the vasculature in a mouse model of pulmonary infection. Our results indicate that A. baumannii uses a two-component receptor system for the acquisition of heme from host heme reservoirs. A Slam-dependent hemophore contributes to heme acquisition in the bacterial pathogen Acinetobacter baumannii.,Bateman TJ, Shah M, Ho TP, Shin HE, Pan C, Harris G, Fegan JE, Islam EA, Ahn SK, Hooda Y, Gray-Owen SD, Chen W, Moraes TF Nat Commun. 2021 Nov 1;12(1):6270. doi: 10.1038/s41467-021-26545-9. PMID:34725337 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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