4cic: Difference between revisions
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==T. potens IscR== | ==T. potens IscR== | ||
<StructureSection load='4cic' size='340' side='right' caption='[[4cic]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='4cic' size='340' side='right'caption='[[4cic]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4cic]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CIC OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4cic]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermincola_potens_JR Thermincola potens JR] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CIC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CIC FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | ||
<tr><td class="sblockLbl"><b>[[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4cic FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cic OCA], [https://pdbe.org/4cic PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cic RCSB], [https://www.ebi.ac.uk/pdbsum/4cic PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cic ProSAT]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/D5X843_THEPJ D5X843_THEPJ] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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The unique regulation of iron-sulfur cluster biogenesis in a Gram-positive bacterium.,Santos JA, Alonso-Garcia N, Macedo-Ribeiro S, Pereira PJ Proc Natl Acad Sci U S A. 2014 May 20. pii: 201322728. PMID:24847070<ref>PMID:24847070</ref> | The unique regulation of iron-sulfur cluster biogenesis in a Gram-positive bacterium.,Santos JA, Alonso-Garcia N, Macedo-Ribeiro S, Pereira PJ Proc Natl Acad Sci U S A. 2014 May 20. pii: 201322728. PMID:24847070<ref>PMID:24847070</ref> | ||
From | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4cic" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: | [[Category: Thermincola potens JR]] | ||
[[Category: | [[Category: Macedo-Ribeiro S]] | ||
[[Category: Pereira PJB]] | |||
[[Category: | [[Category: Santos JA]] | ||
[[Category: | |||
Latest revision as of 14:12, 9 May 2024
T. potens IscRT. potens IscR
Structural highlights
FunctionPublication Abstract from PubMedIron-sulfur clusters function as cofactors of a wide range of proteins, with diverse molecular roles in both prokaryotic and eukaryotic cells. Dedicated machineries assemble the clusters and deliver them to the final acceptor molecules in a tightly regulated process. In the prototypical Gram-negative bacterium Escherichia coli, the two existing iron-sulfur cluster assembly systems, iron-sulfur cluster (ISC) and sulfur assimilation (SUF) pathways, are closely interconnected. The ISC pathway regulator, IscR, is a transcription factor of the helix-turn-helix type that can coordinate a [2Fe-2S] cluster. Redox conditions and iron or sulfur availability modulate the ligation status of the labile IscR cluster, which in turn determines a switch in DNA sequence specificity of the regulator: cluster-containing IscR can bind to a family of gene promoters (type-1) whereas the clusterless form recognizes only a second group of sequences (type-2). However, iron-sulfur cluster biogenesis in Gram-positive bacteria is not so well characterized, and most organisms of this group display only one of the iron-sulfur cluster assembly systems. A notable exception is the unique Gram-positive dissimilatory metal reducing bacterium Thermincola potens, where genes from both systems could be identified, albeit with a diverging organization from that of Gram-negative bacteria. We demonstrated that one of these genes encodes a functional IscR homolog and is likely involved in the regulation of iron-sulfur cluster biogenesis in T. potens. Structural and biochemical characterization of T. potens and E. coli IscR revealed a strikingly similar architecture and unveiled an unforeseen conservation of the unique mechanism of sequence discrimination characteristic of this distinctive group of transcription regulators. The unique regulation of iron-sulfur cluster biogenesis in a Gram-positive bacterium.,Santos JA, Alonso-Garcia N, Macedo-Ribeiro S, Pereira PJ Proc Natl Acad Sci U S A. 2014 May 20. pii: 201322728. PMID:24847070[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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