4hh3: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[4hh3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides] and [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides_2.4.1 Cereibacter sphaeroides 2.4.1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HH3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HH3 FirstGlance]. <br>
-</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=4hh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hh3 OCA], [https://pdbe.org/4hh3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hh3 RCSB], [https://www.ebi.ac.uk/pdbsum/4hh3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hh3 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</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=4hh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hh3 OCA], [https://pdbe.org/4hh3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hh3 RCSB], [https://www.ebi.ac.uk/pdbsum/4hh3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hh3 ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/Q3J179_CERS4 Q3J179_CERS4]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The anoxygenic phototrophic bacterium Rhodobacter sphaeroides uses different energy sources, depending on environmental conditions including aerobic respiration or, in the absence of oxygen, photosynthesis. Photosynthetic genes are repressed at high oxygen tension, but at intermediate levels their partial expression prepares the bacterium for using light energy. Illumination, however, enhances repression under semiaerobic conditions. Here, we describe molecular details of two proteins mediating oxygen and light control of photosynthesis-gene expression: the light-sensing antirepressor AppA and the transcriptional repressor PpsR. Our crystal structures of both proteins and their complex and hydrogen/deuterium-exchange data show that light activation of AppA-PpsR2 affects the PpsR effector region within the complex. DNA binding studies demonstrate the formation of a light-sensitive ternary AppA-PpsR-DNA complex. We discuss implications of these results for regulation by light and oxygen, highlighting new insights into blue light-mediated signal transduction.
-A ternary AppA-PpsR-DNA complex mediates light regulation of photosynthesis-related gene expression.,Winkler A, Heintz U, Lindner R, Reinstein J, Shoeman RL, Schlichting I Nat Struct Mol Biol. 2013 Jul;20(7):859-67. doi: 10.1038/nsmb.2597. Epub 2013 Jun, 2. PMID:23728293<ref>PMID:23728293</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4hh3" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[AppA protein BLUF domain|AppA protein BLUF domain]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>