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==Crystal structure of heme sensor protein PefR in complex with heme and carbon monoxide==
<StructureSection load='7dvt' size='340' side='right'caption='[[7dvt]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DVT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DVT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.09&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=7dvt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dvt OCA], [https://pdbe.org/7dvt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dvt RCSB], [https://www.ebi.ac.uk/pdbsum/7dvt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dvt ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Hemes (iron-porphyrins) are critical for biological processes in all organisms. Hemolytic bacteria survive by acquiring b-type heme from hemoglobin in red blood cells from their animal hosts. These bacteria avoid the cytotoxicity of excess heme during hemolysis by expressing heme-responsive sensor proteins that act as transcriptional factors to regulate the heme efflux system in response to the cellular heme concentration. Here, the underlying regulatory mechanisms were investigated using crystallographic, spectroscopic, and biochemical studies to understand the structural basis of the heme-responsive sensor protein PefR from Streptococcus agalactiae, a causative agent of neonatal life-threatening infections. Structural comparison of heme-free PefR, its complex with a target DNA, and heme-bound PefR revealed that unique heme coordination controls a &gt;20 A structural rearrangement of the DNA binding domains to dissociate PefR from the target DNA. We also found heme-bound PefR stably binds exogenous ligands, including carbon monoxide, a by-product of the heme degradation reaction.

Heme controls the structural rearrangement of its sensor protein mediating the hemolytic bacterial survival.,Nishinaga M, Sugimoto H, Nishitani Y, Nagai S, Nagatoishi S, Muraki N, Tosha T, Tsumoto K, Aono S, Shiro Y, Sawai H Commun Biol. 2021 Apr 13;4(1):467. doi: 10.1038/s42003-021-01987-5. PMID:33850260<ref>PMID:33850260</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 7dvt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Nagai S]]
[[Category: Nishinaga M]]
[[Category: Nishitani Y]]
[[Category: Sawai H]]
[[Category: Shiro Y]]
[[Category: Sugimoto H]]