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| | <StructureSection load='4chu' size='340' side='right'caption='[[4chu]], [[Resolution|resolution]] 2.49Å' scene=''> | | <StructureSection load='4chu' size='340' side='right'caption='[[4chu]], [[Resolution|resolution]] 2.49Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4chu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CHU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CHU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4chu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CHU FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cic|4cic]]</td></tr> | + | </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=4chu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4chu OCA], [https://pdbe.org/4chu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4chu RCSB], [https://www.ebi.ac.uk/pdbsum/4chu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4chu ProSAT]</span></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=4chu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4chu OCA], [http://pdbe.org/4chu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4chu RCSB], [http://www.ebi.ac.uk/pdbsum/4chu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4chu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/C3SZN7_ECOLX C3SZN7_ECOLX]] Regulates the transcription of several operons and genes involved in the biogenesis of Fe-S clusters and Fe-S-containing proteins (By similarity).[HAMAP-Rule:MF_01176] | + | [[https://www.uniprot.org/uniprot/C3SZN7_ECOLX C3SZN7_ECOLX]] Regulates the transcription of several operons and genes involved in the biogenesis of Fe-S clusters and Fe-S-containing proteins (By similarity).[HAMAP-Rule:MF_01176] |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Iron-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.
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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>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 4chu" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Macedo-Ribeiro, S]] | + | [[Category: Macedo-Ribeiro S]] |
| - | [[Category: Pereira, P J.B]] | + | [[Category: Pereira PJB]] |
| - | [[Category: Santos, J A]] | + | [[Category: Santos JA]] |
| - | [[Category: Dna recognition]]
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| - | [[Category: Helix-turn-helix motif]]
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| - | [[Category: Rrf2-like regulator]]
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| - | [[Category: Transcription]]
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| - | [[Category: Transcription regulation]]
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