5dh2: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
 
(3 intermediate revisions by the same user not shown)
Line 1: Line 1:
==Structure of the siderophore periplasmic binding protein from the fuscachelin gene cluster of Thermobifida fusca in I222==
==Structure of the siderophore periplasmic binding protein from the fuscachelin gene cluster of Thermobifida fusca in I222==
<StructureSection load='5dh2' size='340' side='right' caption='[[5dh2]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
<StructureSection load='5dh2' size='340' side='right'caption='[[5dh2]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5dh2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DH2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DH2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5dh2]] is a 2 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=5DH2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DH2 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dh0|5dh0]], [[5dh1|5dh1]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.59&#8491;</td></tr>
<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=5dh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dh2 OCA], [http://pdbe.org/5dh2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dh2 RCSB], [http://www.ebi.ac.uk/pdbsum/5dh2 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5dh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dh2 OCA], [https://pdbe.org/5dh2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dh2 RCSB], [https://www.ebi.ac.uk/pdbsum/5dh2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dh2 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q47NS2_THEFY Q47NS2_THEFY]
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<ref>PMID:26537767</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5dh2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bruner, S D]]
[[Category: Large Structures]]
[[Category: Li, K]]
[[Category: Thermobifida fusca YX]]
[[Category: Fuscachelin]]
[[Category: Bruner SD]]
[[Category: Periplasmic binding protein]]
[[Category: Li K]]
[[Category: Protein binding]]
[[Category: Siderophore]]

Latest revision as of 12:24, 6 March 2024

Structure of the siderophore periplasmic binding protein from the fuscachelin gene cluster of Thermobifida fusca in I222

5dh2, resolution 2.59Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=5dh2&oldid=4080462"