4hf2
From Proteopedia
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| - | + | ==Crystal Structure of E43A IscR mutant bound to its promoter==  | |
| - | + | <StructureSection load='4hf2' size='340' side='right' caption='[[4hf2]], [[Resolution|resolution]] 2.99Å' scene=''>  | |
| - | + | == Structural highlights ==  | |
| + | <table><tr><td colspan='2'>[[4hf2]] is a 4 chain structure with sequence from [http://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=4HF2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HF2 FirstGlance]. <br>  | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hf0|4hf0]], [[4hf1|4hf1]]</td></tr>  | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">iscR, yfhP, b2531, JW2515 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</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=4hf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hf2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hf2 RCSB], [http://www.ebi.ac.uk/pdbsum/4hf2 PDBsum]</span></td></tr>  | ||
| + | </table>  | ||
| + | <div style="background-color:#fffaf0;">  | ||
| + | == Publication Abstract from PubMed ==  | ||
| + | IscR from Escherichia coli is an unusual metalloregulator in that both apo and iron sulfur (Fe-S)-IscR regulate transcription and exhibit different DNA binding specificities. Here, we report structural and biochemical studies of IscR suggesting that remodeling of the protein-DNA interface upon Fe-S ligation broadens the DNA binding specificity of IscR from binding the type 2 motif only to both type 1 and type 2 motifs. Analysis of an apo-IscR variant with relaxed target-site discrimination identified a key residue in wild-type apo-IscR that, we propose, makes unfavorable interactions with a type 1 motif. Upon Fe-S binding, these interactions are apparently removed, thereby allowing holo-IscR to bind both type 1 and type 2 motifs. These data suggest a unique mechanism of ligand-mediated DNA site recognition, whereby metallocluster ligation relocates a protein-specificity determinant to expand DNA target-site selection, allowing a broader transcriptomic response by holo-IscR.  | ||
| - | + | Studies of IscR reveal a unique mechanism for metal-dependent regulation of DNA binding specificity.,Rajagopalan S, Teter SJ, Zwart PH, Brennan RG, Phillips KJ, Kiley PJ Nat Struct Mol Biol. 2013 Jun;20(6):740-7. doi: 10.1038/nsmb.2568. Epub 2013 May , 5. PMID:23644595<ref>PMID:23644595</ref>  | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>  | |
| - | + | </div>  | |
| - | + | == References ==  | |
| - | ==  | + | <references/>  | 
| - | + | __TOC__  | |
| + | </StructureSection>  | ||
[[Category: Escherichia coli k-12]]  | [[Category: Escherichia coli k-12]]  | ||
| - | [[Category: Phillips, K J  | + | [[Category: Phillips, K J]]  | 
| - | [[Category: Rajagopalan, S R  | + | [[Category: Rajagopalan, S R]]  | 
[[Category: Dna binding]]  | [[Category: Dna binding]]  | ||
[[Category: Iron-sulfur cluster]]  | [[Category: Iron-sulfur cluster]]  | ||
Revision as of 12:36, 21 December 2014
Crystal Structure of E43A IscR mutant bound to its promoter
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