6om5

Structure of a haemophore from Haemophilus haemolyticus

spinqualitylabelsall models 6om5, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6om5 is a 1 chain structure with sequence from Haemophilus haemolyticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: CL, GOL, HEM, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0M3G7Q5_HAEHA Publication Abstract from PubMed Commensal bacteria serve as an important line of defense against colonisation by opportunisitic pathogens, but the underlying molecular mechanisms remain poorly explored. Here, we show that strains of a commensal bacterium, Haemophilus haemolyticus, make hemophilin, a heme-binding protein that inhibits growth of the opportunistic pathogen, non-typeable Haemophilus influenzae (NTHi) in culture. We purified the NTHi-inhibitory protein from H. haemolyticus and identified the hemophilin gene using proteomics and a gene knockout. An x-ray crystal structure of recombinant hemophilin shows that the protein does not belong to any of the known heme-binding protein folds, suggesting that it evolved independently. Biochemical characterisation shows that heme can be captured in the ferrous or ferric state, and with a variety of small heme-ligands bound, suggesting that hemophilin could function under a range of physiological conditions. Hemophilin knockout bacteria show a limited capacity to utilise free heme for growth. Our data suggest that hemophilin is a hemophore and that inhibition of NTHi occurs by heme starvation, raising the possibility that competition from hemophilin-producing H. haemolyticus could antagonise NTHi colonisation in the respiratory tract. A heme-binding protein produced by Haemophilus haemolyticus inhibits non-typeable Haemophilus influenzae.,Latham RD, Torrado M, Atto B, Walshe JL, Wilson R, Guss JM, Mackay JP, Tristram S, Gell DA Mol Microbiol. 2019 Nov 19. doi: 10.1111/mmi.14426. PMID:31742788 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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