4nnp

Crystal Structure of Apo Manganese ABC transporter MntC from Staphylococcus aureus bound to an antagonistic fab fragment

spinqualitylabelsall models 4nnp, resolution 2.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4nnp is a 6 chain structure with sequence from Homo sapiens and Staphylococcus aureus subsp. aureus Mu50. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H3JTS7_STAAM Publication Abstract from PubMed Bacterial ATP-binding cassette (ABC) importers play critical roles in nutrient acquisition and are potential antibacterial targets. However, structural bases for their inhibition are poorly defined. These pathways typically rely on substrate binding proteins (SBPs), which are essential for substrate recognition, delivery, and transporter function. We report the crystal structure of a Staphylococcus aureus SBP for Mn(II), termed MntC, in complex with FabC1, a potent antibody inhibitor of the MntABC pathway. This pathway is essential and highly expressed during S. aureus infection and facilitates the import of Mn(II), a critical cofactor for enzymes that detoxify reactive oxygen species (ROS). Structure-based functional studies indicate that FabC1 sterically blocks a structurally conserved surface of MntC, preventing its interaction with the MntB membrane importer and increasing wild-type S. aureus sensitivity to oxidative stress by more than 10-fold. The results define an SBP blocking mechanism as the basis for ABC importer inhibition by an engineered antibody fragment. Structural analysis of bacterial ABC transporter inhibition by an antibody fragment.,Ahuja S, Rouge L, Swem DL, Sudhamsu J, Wu P, Russell SJ, Alexander MK, Tam C, Nishiyama M, Starovasnik MA, Koth CM Structure. 2015 Apr 7;23(4):713-23. doi: 10.1016/j.str.2015.01.020. Epub 2015 Mar, 5. PMID:25752540 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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