1sbp: Difference between revisions

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-[[Image:1sbp.gif|left|200px]]<br /><applet load="1sbp" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1sbp, resolution 1.7&Aring;" />
-'''1.7 ANGSTROMS REFINED STRUCTURE OF SULFATE-BINDING PROTEIN INVOLVED IN ACTIVE TRANSPORT AND NOVEL MODE OF SULFATE BINDING'''<br />
-==Overview==
+==1.7 ANGSTROMS REFINED STRUCTURE OF SULFATE-BINDING PROTEIN INVOLVED IN ACTIVE TRANSPORT AND NOVEL MODE OF SULFATE BINDING==
-Electrostatic interactions are among the key factors determining the structure and function of proteins. Here we report experimental results that illuminate the functional importance of local dipoles to these interactions. The refined 1.7-A X-ray structure of the liganded form of the sulfate-binding protein, a primary sulfate active transport receptor of Salmonella typhimurium, shows that the sulfate dianion is completely buried and bound by hydrogen bonds (mostly main-chain peptide NH groups) and van der Waals forces. The sulfate is also closely linked, via one of these peptide units, to a His residue. It is also adjacent to the N-termini of three alpha-helices, of which the two shortest have their C-termini "capped" by Arg residues. Site-directed mutagenesis of the recombinant Escherichia coli sulfate receptor had no effect on sulfate-binding activity when an Asn residue was substituted for the positively charged His and the two Arg (changed singly and together) residues. These results, combined with other observations, further solidify the idea that stabilization of uncompensated charges in a protein is a highly localized process that involves a collection of local dipoles, including those of peptide units confined to the first turns of helices. The contribution of helix macrodipoles appears insignificant.
+<StructureSection load='1sbp' size='340' side='right'caption='[[1sbp]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+== Structural highlights ==
-==About this Structure==
+<table><tr><td colspan='2'>[[1sbp]] is a 1 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=1SBP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SBP FirstGlance]. <br>
-SBP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SBP OCA].
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
+<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>
-==Reference==
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sbp OCA], [https://pdbe.org/1sbp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sbp RCSB], [https://www.ebi.ac.uk/pdbsum/1sbp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sbp ProSAT]</span></td></tr>
-Dominant role of local dipoles in stabilizing uncompensated charges on a sulfate sequestered in a periplasmic active transport protein., He JJ, Quiocho FA, Protein Sci. 1993 Oct;2(10):1643-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8251939 8251939]
+</table>
-[[Category: Salmonella typhimurium]]
+== Function ==
-[[Category: Single protein]]
+[https://www.uniprot.org/uniprot/SUBI_SALTY SUBI_SALTY] This protein specifically binds sulfate and is involved in its transmembrane transport.
-[[Category: Quiocho, F A.]]
+== Evolutionary Conservation ==
-[[Category: Sack, J S.]]
+[[Image:Consurf_key_small.gif|200px|right]]
-[[Category: SO4]]
+Check<jmol>
-[[Category: binding protein]]
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sb/1sbp_consurf.spt"</scriptWhenChecked>
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:59:49 2008''
+    <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=1sbp ConSurf].
+<div style="clear:both"></div>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
+[[Category: Quiocho FA]]
+[[Category: Sack JS]]