4m1v: Difference between revisions

Latest revision as of 16:30, 20 September 2023

Crystal structure of the ancestral soluble variant of the Human Phosphate Binding Protein (HPBP)

Structural highlights

4m1v is a 1 chain structure with sequence from Unidentified prokaryotic organism. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.3Å
Ligands:	ACT, EDO, GOL, PO4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

PHBP_UNKP May be involved in atherosclerosis.

Function

PHBP_UNKP Phosphate-binding protein.^[1]

Publication Abstract from PubMed

Stable 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.

References

↑ Diemer H, Elias M, Renault F, Rochu D, Contreras-Martel C, Schaeffer C, Van Dorsselaer A, Chabriere E. Tandem use of X-ray crystallography and mass spectrometry to obtain ab initio the complete and exact amino acids sequence of HPBP, a human 38-kDa apolipoprotein. Proteins. 2008 Jun;71(4):1708-20. PMID:18076037 doi:10.1002/prot.21866
↑ Gonzalez D, Hiblot J, Darbinian N, Miller JC, Gotthard G, Amini S, Chabriere E, Elias M. Ancestral mutations as a tool for solubilizing proteins: The case of a hydrophobic phosphate-binding protein. FEBS Open Bio. 2014 Jan 3;4:121-7. doi: 10.1016/j.fob.2013.12.006. eCollection, 2014. PMID:24490136 doi:https://dx.doi.org/10.1016/j.fob.2013.12.006

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Diemer H, Elias M, Renault F, Rochu D, Contreras-Martel C, Schaeffer C, Van Dorsselaer A, Chabriere E. Tandem use of X-ray crystallography and mass spectrometry to obtain ab initio the complete and exact amino acids sequence of HPBP, a human 38-kDa apolipoprotein. Proteins. 2008 Jun;71(4):1708-20. PMID:18076037 doi:10.1002/prot.21866

[2] Gonzalez D, Hiblot J, Darbinian N, Miller JC, Gotthard G, Amini S, Chabriere E, Elias M. Ancestral mutations as a tool for solubilizing proteins: The case of a hydrophobic phosphate-binding protein. FEBS Open Bio. 2014 Jan 3;4:121-7. doi: 10.1016/j.fob.2013.12.006. eCollection, 2014. PMID:24490136 doi:https://dx.doi.org/10.1016/j.fob.2013.12.006

[1]

[2]

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <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" 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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</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>
 </table>

4m1v: Difference between revisions

Latest revision as of 16:30, 20 September 2023

Crystal structure of the ancestral soluble variant of the Human Phosphate Binding Protein (HPBP)

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

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