1qui

From Proteopedia

(Difference between revisions)

Revision as of 09:22, 29 September 2021

PHOSPHATE-BINDING PROTEIN MUTANT WITH ASP 137 REPLACED BY GLY COMPLEX WITH BROMINE AND PHOSPHATE

Structural highlights

1qui is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PSTS_ECOLI] Part of the ABC transporter complex PstSACB involved in phosphate import.

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 forces determining the structure and function of proteins. These are exemplified in the liganded form of the receptor, a phosphate binding protein from Escherichia coli. The phosphate, completely dehydrated and buried in the receptor, is bound by 12 hydrogen bonds as well as a salt link with Arg 135. We have modulated the ionic attraction while preserving the hydrogen bonds by mutating Asp 137, also salt linked to Arg 135, to Asn, Gly or Thr. High-resolution crystallographic analysis revealed that Gly and Thr (but not Asn) mutant proteins have incorporated a more electronegative Cl- in place of the Asp carboxylate. That no dramatic effect on phosphate affinity was produced by these ionic perturbations indicates a major role for hydrogen bonds and other local dipoles in the binding and charge stabilization of ionic ligands.

Modulation of a salt link does not affect binding of phosphate to its specific active transport receptor.,Yao N, Ledvina PS, Choudhary A, Quiocho FA Biochemistry. 1996 Feb 20;35(7):2079-85. PMID:8652549^[1]

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

References

↑ Yao N, Ledvina PS, Choudhary A, Quiocho FA. Modulation of a salt link does not affect binding of phosphate to its specific active transport receptor. Biochemistry. 1996 Feb 20;35(7):2079-85. PMID:8652549 doi:http://dx.doi.org/10.1021/bi952686r

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='1qui' size='340' side='right'caption='[[1qui]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1qui]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QUI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QUI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1qui]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QUI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QUI FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qui OCA], [http://pdbe.org/1qui PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qui RCSB], [http://www.ebi.ac.uk/pdbsum/1qui PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qui ProSAT]</span></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=1qui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qui OCA], [https://pdbe.org/1qui PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qui RCSB], [https://www.ebi.ac.uk/pdbsum/1qui PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qui ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PSTS_ECOLI PSTS_ECOLI]] Part of the ABC transporter complex PstSACB involved in phosphate import.
+[[https://www.uniprot.org/uniprot/PSTS_ECOLI PSTS_ECOLI]] Part of the ABC transporter complex PstSACB involved in phosphate import.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1qui

From Proteopedia

Revision as of 09:22, 29 September 2021

PHOSPHATE-BINDING PROTEIN MUTANT WITH ASP 137 REPLACED BY GLY COMPLEX WITH BROMINE AND PHOSPHATE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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