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==Crystal structure of the sensor domain of the transcriptional regulator HcpR from Porphyromonas Gingivalis==
<StructureSection load='6np6' size='340' side='right'caption='[[6np6]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6np6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_33277 Atcc 33277]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5v3e 5v3e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NP6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NP6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CBG53_06810, PGIN_13-1_00953 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=837 ATCC 33277])</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=6np6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6np6 OCA], [https://pdbe.org/6np6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6np6 RCSB], [https://www.ebi.ac.uk/pdbsum/6np6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6np6 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Although the HcpR regulator plays a vital step in initiation of the nitrosative stress response in many Gram-negative anaerobic bacteria, the molecular mechanisms that it uses to mediate gas sensing are not well understood. Here, a 2.6 A resolution crystal structure of the N-terminal sensing domain of the anaerobic periodontopathogen Porphyromonas gingivalis HcpR is presented. The protein has classical features of the regulators belonging to the FNR-CRP family and contains a hydrophobic pocket in its N-terminal sensing domain. It is shown that heme bound to HcpR exhibits heme iron as a hexacoordinate system in the absence of nitric oxide (NO) and that upon nitrosylation it transitions to a pentacoordinate system. Finally, small-angle X-ray scattering experiments on full-length HcpR reveal that the C-terminal DNA-binding domain of HcpR has a high degree of interdomain flexibility.

Nitrosative stress sensing in Porphyromonas gingivalis: structure of and heme binding by the transcriptional regulator HcpR.,Belvin BR, Musayev FN, Burgner J, Scarsdale JN, Escalante CR, Lewis JP Acta Crystallogr D Struct Biol. 2019 Apr 1;75(Pt 4):437-450. doi:, 10.1107/S205979831900264X. Epub 2019 Apr 5. PMID:30988260<ref>PMID:30988260</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6np6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Atcc 33277]]
[[Category: Large Structures]]
[[Category: Belvin, B R]]
[[Category: Escalante, C R]]
[[Category: Lewis, J P]]
[[Category: Musayev, F N]]
[[Category: Scarsdale, J N]]
[[Category: Turner, J]]
[[Category: Beta barrel]]
[[Category: Dimerization helix]]
[[Category: Heme binding protein]]
[[Category: Transcription]]
[[Category: Transcriptional regulator]]