5dh0

Structure of the siderophore periplasmic binding protein from the fuscachelin gene cluster of Thermobifida fusca in P41

spinqualitylabelsall models 5dh0, resolution 2.44Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5dh0 is a 2 chain structure with sequence from Thefy. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 5dh1, 5dh2 Gene: Tfu_1864 (THEFY) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Iron acquisition is a complex, multicomponent process critical for most organisms' survival and virulence. Small iron chelating molecules, siderophores, mediate transport as key components of common pathways for iron assimilation in many microorganisms. The chemistry and biology of the extraordinary tight and specific metal binding siderophores is of general interest in terms of host/guest chemistry and is a potential target toward the development of therapeutic treatments for microbial virulence. The siderophore pathway of the moderate thermophile, Thermobifida fusca, is an excellent model system to study the process in Gram-positive bacteria. Here we describe the structure and characterization of the siderophore periplasmic binding protein, FscJ from the fuscachelin gene cluster of T. fusca. The structure shows a di-domain arrangement connected with a long alpha-helix hinge. Several X-ray structures detail ligand-free conformational changes at different pH values, illustrating complex interdomain flexibility of the siderophore receptors. We demonstrated that FscJ has a unique recognition mechanism and details the binding interaction with ferric-fuscachelin A through ITC and docking analysis. The presented work provides a structural basis for the complex molecular mechanisms of siderophore recognition and transportation. This article is protected by copyright. All rights reserved. Structure and functional analysis of the siderophore periplasmic binding protein from the fuscachelin gene cluster of Thermobifida fusca.,Li K, Bruner SD Proteins. 2015 Nov 4. doi: 10.1002/prot.24959. PMID:26537767 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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