3vtm | pdb_00003vtm

Structure of heme transport protein IsdH-NEAT3 from S. aureus in complex with Indium-porphyrin

spinqualitylabelsall models 3vtm, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vtm is a 2 chain structure with sequence from Staam. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 3ZZ, GOL Related: 3qug, 3quh, 2e7d, 2z6f Gene: harA, isdH, IsdH-NEAT3, sasI, SAV1731 (STAAM) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ISDH_STAAM] Binds human plasma haptoglobin-hemoglobin complexes, haptoglobin and hemoglobin. Binds haptoglobin-hemoglobin complexes with significantly higher affinity than haptoglobin alone (By similarity). Publication Abstract from PubMed The Isd (iron-regulated surface determinant) system of the human pathogen Staphylococcus aureus is responsible for the acquisition of heme from the host organism. We recently reported that the extracellular heme receptor IsdH-NEAT3 captures and transfers noniron antimicrobial porphyrins containing metals in oxidation state (III). However, it is unclear if geometric factors such as the size of the metal (ionic radius) affect binding and transfer of metalloporphyrins. We carried out an ample structural, functional, and thermodynamic analysis of the binding properties of antimicrobial indium(III)-porphyrin, which bears a much larger metal ion than the iron(III) of the natural ligand heme. The results demonstrate that the NEAT3 receptor recognizes the In(III)-containing PPIX in a manner very similar to that of heme. Site-directed mutagenesis identifies Tyr642 as the central element in the recognition mechanism as suggested from the crystal structures. Importantly, the NEAT3 receptor possesses the remarkable ability to capture dimers of metalloporphyrin. Molecular dynamics simulations reveal that IsdH-NEAT3 does not require conformational changes, or large rearrangements of the residues within its binding site, to accommodate the much larger (heme)2 ligand. We discuss the implications of these findings for the design of potent inhibitors against this family of key receptors of S. aureus. Selective binding of antimicrobial porphyrins to the heme-receptor IsdH-NEAT3 of Staphylococcus aureus.,Vu NT, Moriwaki Y, Caaveiro JM, Terada T, Tsutsumi H, Hamachi I, Shimizu K, Tsumoto K Protein Sci. 2013 Jul;22(7):942-53. doi: 10.1002/pro.2276. Epub 2013 Jun 6. PMID:23649633 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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