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5dh1

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==Structure of the siderophore periplasmic binding protein from the fuscachelin gene cluster of Thermobifida fusca in P21==
==Structure of the siderophore periplasmic binding protein from the fuscachelin gene cluster of Thermobifida fusca in P21==
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<StructureSection load='5dh1' size='340' side='right' caption='[[5dh1]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
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<StructureSection load='5dh1' size='340' side='right'caption='[[5dh1]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5dh1]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DH1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DH1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5dh1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca_YX Thermobifida fusca YX]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DH1 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dh0|5dh0]], [[5dh2|5dh2]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.842&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5dh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dh1 OCA], [http://pdbe.org/5dh1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dh1 RCSB], [http://www.ebi.ac.uk/pdbsum/5dh1 PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5dh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dh1 OCA], [https://pdbe.org/5dh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dh1 RCSB], [https://www.ebi.ac.uk/pdbsum/5dh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dh1 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q47NS2_THEFY Q47NS2_THEFY]
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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.
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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<ref>PMID:26537767</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5dh1" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bruner, S D]]
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[[Category: Large Structures]]
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[[Category: Li, K]]
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[[Category: Thermobifida fusca YX]]
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[[Category: Fuscachelin]]
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[[Category: Bruner SD]]
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[[Category: Periplasmic binding protein]]
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[[Category: Li K]]
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[[Category: Protein binding]]
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[[Category: Siderophore]]
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Current revision

Structure of the siderophore periplasmic binding protein from the fuscachelin gene cluster of Thermobifida fusca in P21

PDB ID 5dh1

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