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1sbp

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Revision as of 20:40, 10 September 2015

1.7 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. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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.

Publication Abstract from PubMed

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.

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:8251939^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ He JJ, Quiocho FA. Dominant role of local dipoles in stabilizing uncompensated charges on a sulfate sequestered in a periplasmic active transport protein. Protein Sci. 1993 Oct;2(10):1643-7. PMID:8251939

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1sbp"

Categories: Quiocho, F A | Sack, J S | Binding protein

@@ Line 2: / Line 2: @@
 <StructureSection load='1sbp' size='340' side='right' caption='[[1sbp]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1sbp]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SBP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1sbp]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SBP FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sbp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1sbp RCSB], [http://www.ebi.ac.uk/pdbsum/1sbp PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sbp OCA], [http://pdbe.org/1sbp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sbp RCSB], [http://www.ebi.ac.uk/pdbsum/1sbp PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1sbp" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
 [[Category: Quiocho, F A]]
 [[Category: Sack, J S]]
 [[Category: Binding protein]]

1sbp

From Proteopedia

Revision as of 20:40, 10 September 2015

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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