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1pbp

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[[Image:1pbp.jpg|left|200px]]
 
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{{Structure
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==FINE TUNING OF THE SPECIFICITY OF THE PERIPLASMIC PHOSPHATE TRANSPORT RECEPTOR: SITE-DIRECTED MUTAGENESIS, LIGAND BINDING, AND CRYSTALLOGRAPHIC STUDIES==
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|PDB= 1pbp |SIZE=350|CAPTION= <scene name='initialview01'>1pbp</scene>, resolution 1.9&Aring;
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<StructureSection load='1pbp' size='340' side='right'caption='[[1pbp]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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<table><tr><td colspan='2'>[[1pbp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PBP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PBP FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pbp OCA], [https://pdbe.org/1pbp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pbp RCSB], [https://www.ebi.ac.uk/pdbsum/1pbp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pbp ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pbp OCA], [http://www.ebi.ac.uk/pdbsum/1pbp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pbp RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/PSTS_ECOLI PSTS_ECOLI] Part of the ABC transporter complex PstSACB involved in phosphate import.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pb/1pbp_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1pbp ConSurf].
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<div style="clear:both"></div>
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'''FINE TUNING OF THE SPECIFICITY OF THE PERIPLASMIC PHOSPHATE TRANSPORT RECEPTOR: SITE-DIRECTED MUTAGENESIS, LIGAND BINDING, AND CRYSTALLOGRAPHIC STUDIES'''
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==See Also==
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*[[Phosphate-binding protein|Phosphate-binding protein]]
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__TOC__
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==Overview==
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</StructureSection>
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Phosphorous, primarily in the form of phosphate, is a critical nutrient for the life of a cell. We have previously determined the 1.7-A resolution structure of the phosphate-binding protein, an initial receptor for the high-affinity phosphate active transport system or permease in Escherichia coli (Luecke, H., and Quiocho, F.A. (1990) Nature 347, 402-406). This structure is the first to reveal the key role of hydrogen bonding interactions in conferring the high specificity of the permease, a specificity also shared by other phosphate transport systems. Both monobasic and dibasic phosphates are recognized by the phosphate-binding protein with Asp56 playing a key role. Here we report site-directed mutagenesis, ligand binding, and crystallographic studies of the binding protein which show that introduction of one additional Asp by mutagenesis of the Thr141 in the ligand-binding site restricts binding to only the monobasic phosphate.
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==About this Structure==
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1PBP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PBP OCA].
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==Reference==
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Fine tuning the specificity of the periplasmic phosphate transport receptor. Site-directed mutagenesis, ligand binding, and crystallographic studies., Wang Z, Choudhary A, Ledvina PS, Quiocho FA, J Biol Chem. 1994 Oct 7;269(40):25091-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7929197 7929197]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Choudhary, A.]]
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[[Category: Choudhary A]]
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[[Category: Ledvina, P S.]]
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[[Category: Ledvina PS]]
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[[Category: Quiocho, F A.]]
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[[Category: Quiocho FA]]
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[[Category: Wang, Z.]]
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[[Category: Wang Z]]
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[[Category: phosphate transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:57:32 2008''
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Current revision

FINE TUNING OF THE SPECIFICITY OF THE PERIPLASMIC PHOSPHATE TRANSPORT RECEPTOR: SITE-DIRECTED MUTAGENESIS, LIGAND BINDING, AND CRYSTALLOGRAPHIC STUDIES

PDB ID 1pbp

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