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== | ==Crystal Structure of the sensor histidine kinase regulator YycI from Bacillus subtitlis== | ||
<StructureSection load='2o3o' size='340' side='right'caption='[[2o3o]], [[Resolution|resolution]] 2.89Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2o3o]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O3O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O3O FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.89Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=2o3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o3o OCA], [https://pdbe.org/2o3o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o3o RCSB], [https://www.ebi.ac.uk/pdbsum/2o3o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o3o ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/YYCI_BACSU YYCI_BACSU] Together with YycH, regulates the activity of the two-component system YycF/YycG.<ref>PMID:17307850</ref> <ref>PMID:18408157</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o3/2o3o_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2o3o ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
YycI and YycH are two membrane-anchored periplasmic proteins that regulate the essential Bacillus subtilis YycG histidine kinase through direct interaction. Here we present the crystal structure of YycI at a 2.9-A resolution. YycI forms a dimer, and remarkably the structure resembles that of the two C-terminal domains of YycH despite nearly undetectable sequence homology (10%) between the two proteins. | YycI and YycH are two membrane-anchored periplasmic proteins that regulate the essential Bacillus subtilis YycG histidine kinase through direct interaction. Here we present the crystal structure of YycI at a 2.9-A resolution. YycI forms a dimer, and remarkably the structure resembles that of the two C-terminal domains of YycH despite nearly undetectable sequence homology (10%) between the two proteins. | ||
The crystal structure of Bacillus subtilis YycI reveals a common fold for two members of an unusual class of sensor histidine kinase regulatory proteins.,Santelli E, Liddington RC, Mohan MA, Hoch JA, Szurmant H J Bacteriol. 2007 Apr;189(8):3290-5. Epub 2007 Feb 16. PMID:17307848<ref>PMID:17307848</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2o3o" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Liddington | [[Category: Liddington RC]] | ||
[[Category: Santelli | [[Category: Santelli E]] | ||
Latest revision as of 08:23, 17 October 2024
Crystal Structure of the sensor histidine kinase regulator YycI from Bacillus subtitlisCrystal Structure of the sensor histidine kinase regulator YycI from Bacillus subtitlis
Structural highlights
FunctionYYCI_BACSU Together with YycH, regulates the activity of the two-component system YycF/YycG.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedYycI and YycH are two membrane-anchored periplasmic proteins that regulate the essential Bacillus subtilis YycG histidine kinase through direct interaction. Here we present the crystal structure of YycI at a 2.9-A resolution. YycI forms a dimer, and remarkably the structure resembles that of the two C-terminal domains of YycH despite nearly undetectable sequence homology (10%) between the two proteins. The crystal structure of Bacillus subtilis YycI reveals a common fold for two members of an unusual class of sensor histidine kinase regulatory proteins.,Santelli E, Liddington RC, Mohan MA, Hoch JA, Szurmant H J Bacteriol. 2007 Apr;189(8):3290-5. Epub 2007 Feb 16. PMID:17307848[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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