1sbp: Difference between revisions

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New page: left|200px<br /><applet load="1sbp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sbp, resolution 1.7Å" /> '''1.7 ANGSTROMS REFINED...
 
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'''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>
1SBP 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 SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.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://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:15:26 2007''
    <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]]

Latest revision as of 11:29, 14 February 2024

1.7 ANGSTROMS REFINED STRUCTURE OF SULFATE-BINDING PROTEIN INVOLVED IN ACTIVE TRANSPORT AND NOVEL MODE OF SULFATE BINDING1.7 ANGSTROMS REFINED STRUCTURE OF SULFATE-BINDING PROTEIN INVOLVED IN ACTIVE TRANSPORT AND NOVEL MODE OF SULFATE BINDING

Structural highlights

1sbp is a 1 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SUBI_SALTY This protein specifically binds sulfate and is involved in its transmembrane transport.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1sbp, resolution 1.70Å

Drag the structure with the mouse to rotate

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