3nr7: Difference between revisions
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==Crystal structure of S. typhimurium H-NS 1-83== | ==Crystal structure of S. typhimurium H-NS 1-83== | ||
<StructureSection load='3nr7' size='340' side='right' caption='[[3nr7]], [[Resolution|resolution]] 3.70Å' scene=''> | <StructureSection load='3nr7' size='340' side='right'caption='[[3nr7]], [[Resolution|resolution]] 3.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3nr7]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3nr7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NR7 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.7Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3nr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nr7 OCA], [https://pdbe.org/3nr7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nr7 RCSB], [https://www.ebi.ac.uk/pdbsum/3nr7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nr7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/HNS_SALTY HNS_SALTY] H-NS binds tightly to ds-DNA, increases its thermal stability and inhibits transcription. It also binds to ss-DNA and RNA but with a much lower affinity. H-NS has possible histone-like function. May be a global transcriptional regulator through its ability to bind to curved DNA sequences, which are found in regions upstream of a certain subset of promoters. It plays a role in the thermal control of pili production. It is subject to transcriptional auto-repression. It binds preferentially to the upstream region of its own gene recognizing two segments of DNA on both sides of a bend centered around -150 (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium]] | ||
[[Category: | [[Category: Arold ST]] | ||
[[Category: | [[Category: Ladbury JE]] | ||
[[Category: | [[Category: Leonard PG]] | ||
[[Category: | [[Category: Parkinson GN]] | ||