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5ydo

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Current revision (10:22, 27 March 2024) (edit) (undo)
 
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<StructureSection load='5ydo' size='340' side='right'caption='[[5ydo]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='5ydo' size='340' side='right'caption='[[5ydo]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ydo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cholerae-suis"_smith_1894 "bacillus cholerae-suis" smith 1894]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YDO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YDO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ydo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YDO FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yjiE_2, A7S24_17855, A7S72_19140, IN36_08870, IN69_18165, NGUA18_03006 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28901 "Bacillus cholerae-suis" Smith 1894])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5ydo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ydo OCA], [http://pdbe.org/5ydo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ydo RCSB], [http://www.ebi.ac.uk/pdbsum/5ydo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ydo 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=5ydo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ydo OCA], [https://pdbe.org/5ydo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ydo RCSB], [https://www.ebi.ac.uk/pdbsum/5ydo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ydo 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/Q7CP75_SALTY Q7CP75_SALTY]
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Hypochlorous acid (HOCl) is generated in the immune system to kill microorganisms. In Escherichia coli, a hypochlorite-specific transcription regulator, HypT, has been characterized. HypT belongs to the LysR-type transcriptional regulator (LTTR) family that contains a DNA-binding domain (DBD) and a regulatory domain (RD). Here, we identified a hypT gene from Salmonella enterica serovar Typhimurium and determined crystal structures of the full-length HypT protein and the RD. The full-length structure reveals a type of tetrameric assembly in the LTTR family. Based on HOCl-bound and oxidation-mimicking structures, we identified a HOCl-driven methionine oxidation mechanism, in which the bound HOCl oxidizes a conserved methionine residue lining the putative ligand-binding site in the RD. Furthermore, we proposed a molecular model for the oxidized HypT, where methionine oxidation by HOCl results in a conformational change of the RD, inducing a counter rotation of the DBD dimers. Target genes that are regulated by HypT and their roles in Salmonella were also investigated. DNase I footprinting experiments revealed a DNA segment containing two pseudopalindromic motifs that are separated by approximately 100 bp, suggesting that only the oxidized structure makes a concomitant binding, forming a DNA loop. An understanding of the HypT-mediated mechanism would be helpful for controlling many pathogenic bacteria by counteracting bacterial HOCl defense mechanisms.
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Structural basis for HOCl recognition and regulation mechanisms of HypT, a hypochlorite-specific transcriptional regulator.,Jo I, Kim D, No T, Hong S, Ahn J, Ryu S, Ha NC Proc Natl Acad Sci U S A. 2019 Feb 26;116(9):3740-3745. doi:, 10.1073/pnas.1811509116. Epub 2019 Feb 7. PMID:30733296<ref>PMID:30733296</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 5ydo" 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: Bacillus cholerae-suis smith 1894]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ahn, J]]
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[[Category: Salmonella enterica]]
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[[Category: Ha, N C]]
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[[Category: Ahn J]]
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[[Category: Hong, S]]
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[[Category: Ha NC]]
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[[Category: Jo, I]]
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[[Category: Hong S]]
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[[Category: Dna binding protein]]
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[[Category: Jo I]]
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[[Category: Hocl]]
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[[Category: Hocl-specific transcription factor]]
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[[Category: Hypochlorite]]
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[[Category: Hypochlorous acid]]
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[[Category: Lysr-type transcription regulator]]
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[[Category: Regulatory domain]]
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Current revision

Regulatory domain of HypT from Salmonella typhimurium (apo-form)

PDB ID 5ydo

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