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| | ==NMR solution structure of crambin in DPC micelles== | | ==NMR solution structure of crambin in DPC micelles== |
| - | <StructureSection load='1yva' size='340' side='right'caption='[[1yva]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1yva' size='340' side='right'caption='[[1yva]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1yva]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Abyssinian_crambe Abyssinian crambe]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YVA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1yva]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Crambe_hispanica_subsp._abyssinica Crambe hispanica subsp. abyssinica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YVA FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1yv8|1yv8]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">THI2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3721 Abyssinian crambe])</td></tr>
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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=1yva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yva OCA], [https://pdbe.org/1yva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yva RCSB], [https://www.ebi.ac.uk/pdbsum/1yva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yva 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=1yva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yva OCA], [https://pdbe.org/1yva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yva RCSB], [https://www.ebi.ac.uk/pdbsum/1yva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yva ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CRAM_CRAAB CRAM_CRAAB]] The function of this hydrophobic plant seed protein is not known.
| + | [https://www.uniprot.org/uniprot/CRAM_CRAAB CRAM_CRAAB] The function of this hydrophobic plant seed protein is not known. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Abyssinian crambe]] | + | [[Category: Crambe hispanica subsp. abyssinica]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ahn, H C]] | + | [[Category: Ahn H-C]] |
| - | [[Category: Markley, J L]] | + | [[Category: Markley JL]] |
| - | [[Category: Crambin]]
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| - | [[Category: Dpc]]
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| - | [[Category: Micelle]]
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| - | [[Category: Plant protein]]
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| Structural highlights
Function
CRAM_CRAAB The function of this hydrophobic plant seed protein is not known.
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
We chose crambin, a hydrophobic and water-insoluble protein originally isolated from the seeds of the plant Crambe abyssinica, as a model for NMR investigations of membrane-associated proteins. We produced isotopically labeled crambin(P22,L25) (variant of crambin containing Pro22 and Leu25) as a cleavable fusion with staphylococcal nuclease and refolded the protein by an approach that has proved successful for the production of proteins with multiple disulfide bonds. We used NMR spectroscopy to determine the three-dimensional structure of the protein in two membrane-mimetic environments: in a mixed aqueous-organic solvent (75%/25%, acetone/water) and in DPC micelles. With the sample in the mixed solvent, it was possible to determine (>NH...OC<) hydrogen bonds directly by the detection of (h3)J(NC)' couplings. H-bonds determined in this manner were utilized in the refinement of the NMR-derived protein structures. With the protein in DPC (dodecylphosphocholine) micelles, we used manganous ion as an aqueous paramagnetic probe to determine the surface of crambin that is shielded by the detergent. With the exception of the aqueous solvent exposed loop containing residues 20 and 21, the protein surface was protected by DPC. This suggests that the protein may be similarly embedded in physiological membranes. The strategy described here for the expression and structure determination of crambin should be applicable to structural and functional studies of membrane active toxins and small membrane proteins.
Three-dimensional structure of the water-insoluble protein crambin in dodecylphosphocholine micelles and its minimal solvent-exposed surface.,Ahn HC, Juranic N, Macura S, Markley JL J Am Chem Soc. 2006 Apr 5;128(13):4398-404. PMID:16569017[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ahn HC, Juranic N, Macura S, Markley JL. Three-dimensional structure of the water-insoluble protein crambin in dodecylphosphocholine micelles and its minimal solvent-exposed surface. J Am Chem Soc. 2006 Apr 5;128(13):4398-404. PMID:16569017 doi:10.1021/ja057773d
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