5DH0

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

Summary for 5DH0

• Entry DOI: 10.2210/pdb5dh0/pdb
• Related: 5DH1 5DH2
• Descriptor: siderophore periplasmic binding protein (2 entities in total)
• Functional Keywords: siderophore, periplasmic binding protein, fuscachelin, protein binding
• Biological source: Thermobifida fusca (strain YX)
• Total number of polymer chains: 2
• Total formula weight: 67470.27

Authors

Li, K.,Bruner, S.D. (deposition date: 2015-08-29, release date: 2015-11-18, Last modification date: 2024-03-06)

Primary citation

Li, K.,Bruner, S.D.
Structure and functional analysis of the siderophore periplasmic binding protein from the fuscachelin gene cluster of Thermobifida fusca.
Proteins, 84:118-128, 2016

PubMed Abstract: 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 α-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.

PubMed: 26537767
DOI: 10.1002/prot.24959

Experimental method

X-RAY DIFFRACTION (2.444 Å)