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3vox

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==X-ray Crystal Structure of Wild Type HrtR in the Apo Form==
==X-ray Crystal Structure of Wild Type HrtR in the Apo Form==
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<StructureSection load='3vox' size='340' side='right' caption='[[3vox]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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<StructureSection load='3vox' size='340' side='right'caption='[[3vox]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3vox]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lacla Lacla]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VOX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VOX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3vox]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis_subsp._lactis_Il1403 Lactococcus lactis subsp. lactis Il1403]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VOX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VOX FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">L53789, LL0661, ygfC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272623 LACLA])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
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<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=3vox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vox OCA], [http://pdbe.org/3vox PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vox RCSB], [http://www.ebi.ac.uk/pdbsum/3vox PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vox ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vox OCA], [https://pdbe.org/3vox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vox RCSB], [https://www.ebi.ac.uk/pdbsum/3vox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vox ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q9CHR1_LACLA Q9CHR1_LACLA]
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Although heme is a crucial element for many biological processes including respiration, heme homeostasis should be regulated strictly due to the cytotoxicity of free heme molecules. Numerous lactic acid bacteria, including Lactococcus lactis, acquire heme molecules exogenously to establish an aerobic respiratory chain. A heme efflux system plays an important role for heme homeostasis to avoid cytotoxicity of acquired free heme, but its regulatory mechanism is not clear. Here, we report that the transcriptional regulator heme-regulated transporter regulator (HrtR) senses and binds a heme molecule as its physiological effector to regulate the expression of the heme-efflux system responsible for heme homeostasis in L. lactis. To elucidate the molecular mechanisms of how HrtR senses a heme molecule and regulates gene expression for the heme efflux system, we determined the crystal structures of the apo-HrtR.DNA complex, apo-HrtR, and holo-HrtR at a resolution of 2.0, 3.1, and 1.9 A, respectively. These structures revealed that HrtR is a member of the TetR family of transcriptional regulators. The residue pair Arg-46 and Tyr-50 plays a crucial role for specific DNA binding through hydrogen bonding and a CH-pi interaction with the DNA bases. HrtR adopts a unique mechanism for its functional regulation upon heme sensing. Heme binding to HrtR causes a coil-to-helix transition of the alpha4 helix in the heme-sensing domain, which triggers a structural change of HrtR, causing it to dissociate from the target DNA for derepression of the genes encoding the heme efflux system. HrtR uses a unique heme-sensing motif with bis-His (His-72 and His-149) ligation to the heme, which is essential for the coil-to-helix transition of the alpha4 helix upon heme sensing.
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Structural Basis for the Transcriptional Regulation of Heme Homeostasis in Lactococcus lactis.,Sawai H, Yamanaka M, Sugimoto H, Shiro Y, Aono S J Biol Chem. 2012 Aug 31;287(36):30755-68. Epub 2012 Jul 13. PMID:22798069<ref>PMID:22798069</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3vox" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Lacla]]
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[[Category: Lactococcus lactis subsp. lactis Il1403]]
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[[Category: Aono, S]]
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[[Category: Large Structures]]
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[[Category: Sawai, H]]
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[[Category: Aono S]]
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[[Category: Shiro, Y]]
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[[Category: Sawai H]]
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[[Category: Sugimoto, H]]
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[[Category: Shiro Y]]
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[[Category: Sensor protein]]
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[[Category: Sugimoto H]]
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[[Category: Tetr superfamily]]
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[[Category: Transcription]]
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Current revision

X-ray Crystal Structure of Wild Type HrtR in the Apo Form

PDB ID 3vox

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