4m1v: Difference between revisions
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<StructureSection load='4m1v' size='340' side='right'caption='[[4m1v]], [[Resolution|resolution]] 1.30Å' scene=''> | <StructureSection load='4m1v' size='340' side='right'caption='[[4m1v]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4m1v]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4m1v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Unidentified_prokaryotic_organism Unidentified prokaryotic organism]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M1V FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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'>[https://proteopedia.org/fgij/fg.htm?mol=4m1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m1v OCA], [https://pdbe.org/4m1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m1v RCSB], [https://www.ebi.ac.uk/pdbsum/4m1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m1v ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Disease == | == Disease == | ||
[ | [https://www.uniprot.org/uniprot/PHBP_UNKP PHBP_UNKP] May be involved in atherosclerosis. | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/PHBP_UNKP PHBP_UNKP] Phosphate-binding protein.<ref>PMID:18076037</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Unidentified prokaryotic organism]] | ||
[[Category: Amini | [[Category: Amini S]] | ||
[[Category: Chabriere | [[Category: Chabriere E]] | ||
[[Category: Darbinian | [[Category: Darbinian N]] | ||
[[Category: Elias | [[Category: Elias M]] | ||
[[Category: Gonzalez | [[Category: Gonzalez D]] | ||
[[Category: Gotthard | [[Category: Gotthard G]] | ||
[[Category: Hiblot | [[Category: Hiblot J]] | ||
[[Category: Miller | [[Category: Miller JS]] | ||
Revision as of 13:47, 21 December 2022
Crystal structure of the ancestral soluble variant of the Human Phosphate Binding Protein (HPBP)Crystal structure of the ancestral soluble variant of the Human Phosphate Binding Protein (HPBP)
Structural highlights
DiseasePHBP_UNKP May be involved in atherosclerosis. FunctionPHBP_UNKP Phosphate-binding protein.[1] Publication Abstract from PubMedStable and soluble proteins are ideal candidates for functional and structural studies. Unfortunately, some proteins or enzymes can be difficult to isolate, being sometimes poorly expressed in heterologous systems, insoluble and/or unstable. Numerous methods have been developed to address these issues, from the screening of various expression systems to the modification of the target protein itself. Here we use a hydrophobic, aggregation-prone, phosphate-binding protein (HPBP) as a case study. We describe a simple and fast method that selectively uses ancestral mutations to generate a soluble, stable and functional variant of the target protein, here named sHPBP. This variant is highly expressed in Escherichia coli, is easily purified and its structure was solved at much higher resolution than its wild-type progenitor (1.3 versus 1.9 A, respectively). Ancestral mutations as a tool for solubilizing proteins: The case of a hydrophobic phosphate-binding protein.,Gonzalez D, Hiblot J, Darbinian N, Miller JC, Gotthard G, Amini S, Chabriere E, Elias M FEBS Open Bio. 2014 Jan 3;4:121-7. doi: 10.1016/j.fob.2013.12.006. eCollection, 2014. PMID:24490136[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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