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| | <StructureSection load='3w9v' size='340' side='right'caption='[[3w9v]], [[Resolution|resolution]] 1.03Å' scene=''> | | <StructureSection load='3w9v' size='340' side='right'caption='[[3w9v]], [[Resolution|resolution]] 1.03Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3w9v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Unkp Unkp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W9V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3w9v]] is a 2 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=3W9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W9V FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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]] 1.031Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2v3q|2v3q]], [[3g62|3g62]], [[2q9t|2q9t]], [[3w9w|3w9w]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=3w9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w9v OCA], [https://pdbe.org/3w9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w9v RCSB], [https://www.ebi.ac.uk/pdbsum/3w9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w9v 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=3w9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w9v OCA], [https://pdbe.org/3w9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w9v RCSB], [https://www.ebi.ac.uk/pdbsum/3w9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w9v ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[https://www.uniprot.org/uniprot/PHBP_UNKP PHBP_UNKP]] May be involved in atherosclerosis.
| + | [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>
| + | [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: Unkp]] | + | [[Category: Unidentified prokaryotic organism]] |
| - | [[Category: Gai, Z Q]] | + | [[Category: Gai ZQ]] |
| - | [[Category: Hirano, N]] | + | [[Category: Hirano N]] |
| - | [[Category: Nakamura, A]] | + | [[Category: Nakamura A]] |
| - | [[Category: Tanaka, I]] | + | [[Category: Tanaka I]] |
| - | [[Category: Tanaka, Y]] | + | [[Category: Tanaka Y]] |
| - | [[Category: Yao, M]] | + | [[Category: Yao M]] |
| - | [[Category: Ding]]
| + | |
| - | [[Category: Phosphate]]
| + | |
| - | [[Category: Phosphate binding apolipoprotein]]
| + | |
| - | [[Category: Refolded]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Disease
PHBP_UNKP May be involved in atherosclerosis.
Function
PHBP_UNKP Phosphate-binding protein.[1]
Publication Abstract from PubMed
After crystallization of a certain protein-RNA complex, well diffracting crystals were obtained. However, the asymmetric unit of the crystal was too small to locate any components. Mass spectrometry and X-ray crystal structure analysis showed that it was a member of the DING protein family (HPBP). Surprisingly, the structure of HPBP reported previously was also determined accidentally as a contaminant, suggesting that HPBP has a strong tendency to crystallize. Furthermore, DING proteins were reported to relate in disease. These observations suggest that DING has potential for application in a wide range of research fields. To enable further analyses, a system for preparation of HPBP was constructed. As HPBP was expressed in insoluble form in Escherichia coli, it was unfolded chemically and refolded. Finally, a very high yield preparation method was constructed, in which 43 mg of HPBP was obtained from 1 L of culture. Furthermore, to evaluate the validity of refolding, its crystal structure was determined at 1.03 A resolution. The determined structure was identical to the native structure, in which two disulfide bonds were recovered correctly and a phosphate ion was captured. Based on these results, it was concluded that the refolded HPBP recovers its structure correctly.
Crystal structure analysis, overexpression and refolding behaviour of a DING protein with single mutation.,Gai Z, Nakamura A, Tanaka Y, Hirano N, Tanaka I, Yao M J Synchrotron Radiat. 2013 Nov;20(Pt 6):854-8. doi: 10.1107/S0909049513020694., Epub 2013 Sep 29. PMID:24121327[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
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
- ↑ Gai Z, Nakamura A, Tanaka Y, Hirano N, Tanaka I, Yao M. Crystal structure analysis, overexpression and refolding behaviour of a DING protein with single mutation. J Synchrotron Radiat. 2013 Nov;20(Pt 6):854-8. doi: 10.1107/S0909049513020694., Epub 2013 Sep 29. PMID:24121327 doi:http://dx.doi.org/10.1107/S0909049513020694
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