2nnc: Difference between revisions
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New page: left|200px<br /><applet load="2nnc" size="350" color="white" frame="true" align="right" spinBox="true" caption="2nnc, resolution 2.140Å" /> '''Structure of the su... |
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== | ==Structure of the sulfur carrier protein SoxY from Chlorobium limicola f thiosulfatophilum== | ||
Dissimilatory oxidation of thiosulfate in the green sulfur bacterium | <StructureSection load='2nnc' size='340' side='right'caption='[[2nnc]], [[Resolution|resolution]] 2.14Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2nnc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlorobium_limicola Chlorobium limicola]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NNC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NNC 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]] 2.14Å</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=HDZ:NITROGEN+MOLECULE'>HDZ</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=2nnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nnc OCA], [https://pdbe.org/2nnc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nnc RCSB], [https://www.ebi.ac.uk/pdbsum/2nnc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nnc ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8RLX2_CHLLI Q8RLX2_CHLLI] | |||
== 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/nn/2nnc_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2nnc ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Dissimilatory oxidation of thiosulfate in the green sulfur bacterium Chlorobium limicola f. thiosulfatophilum is carried out by the ubiquitous sulfur-oxidizing (Sox) multi-enzyme system. In this system, SoxY plays a key role, functioning as the sulfur substrate-binding protein that offers its sulfur substrate, which is covalently bound to a conserved C-terminal cysteine, to another oxidizing Sox enzyme. Here, we report the crystal structures of a stand-alone SoxY protein of C. limicola f. thiosulfatophilum, solved at 2.15 A and 2.40 A resolution using X-ray diffraction data collected at 100 K and room temperature, respectively. The structure reveals a monomeric Ig-like protein, with an N-terminal alpha-helix, that oligomerizes into a tetramer via conserved contact regions between the monomers. The tetramer can be described as a dimer of dimers that exhibits one large hydrophobic contact region in each dimer and two small hydrophilic interface patches in the tetramer. At the tetramer interface patch, two conserved redox-active C-terminal cysteines form an intersubunit disulfide bridge. Intriguingly, SoxY exhibits a dimer/tetramer equilibrium that is dependent on the redox state of the cysteines and on the type of sulfur substrate component bound to them. Taken together, the dimer/tetramer equilibrium, the specific interactions between the subunits in the tetramer, and the significant conservation level of the interfaces strongly indicate that these SoxY oligomers are biologically relevant. | |||
X-ray crystallographic analysis of the sulfur carrier protein SoxY from Chlorobium limicola f. thiosulfatophilum reveals a tetrameric structure.,Stout J, Van Driessche G, Savvides SN, Van Beeumen J Protein Sci. 2007 Apr;16(4):589-601. Epub 2007 Feb 27. PMID:17327392<ref>PMID:17327392</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2nnc" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Chlorobium limicola]] | [[Category: Chlorobium limicola]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Savvides SN]] | |||
[[Category: Stout J]] | |||
[[Category: Savvides | [[Category: Van Beeumen J]] | ||
[[Category: Stout | [[Category: Van Driessche G]] | ||
[[Category: | |||
[[Category: | |||
