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| | ==Bombyx mori lipoprotein 7 isolated from its natural source at 1.33 A resolution== | | ==Bombyx mori lipoprotein 7 isolated from its natural source at 1.33 A resolution== |
| - | <StructureSection load='4efp' size='340' side='right' caption='[[4efp]], [[Resolution|resolution]] 1.33Å' scene=''> | + | <StructureSection load='4efp' size='340' side='right'caption='[[4efp]], [[Resolution|resolution]] 1.33Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4efp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EFP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EFP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4efp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EFP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</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]] 1.33Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=0AF:7-HYDROXY-L-TRYPTOPHAN'>0AF</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0AF:7-HYDROXY-L-TRYPTOPHAN'>0AF</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pub|3pub]], [[4efq|4efq]], [[4efr|4efr]]</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=4efp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4efp OCA], [https://pdbe.org/4efp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4efp RCSB], [https://www.ebi.ac.uk/pdbsum/4efp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4efp ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4efp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4efp OCA], [http://pdbe.org/4efp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4efp RCSB], [http://www.ebi.ac.uk/pdbsum/4efp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4efp ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/E5EVW2_BOMMO E5EVW2_BOMMO] |
| | <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: Bombyx mori]] | | [[Category: Bombyx mori]] |
| - | [[Category: Bujacz, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Bujacz, G]] | + | [[Category: Bujacz A]] |
| - | [[Category: Jaskolski, M]] | + | [[Category: Bujacz G]] |
| - | [[Category: Mueller-Dieckmann, J]] | + | [[Category: Jaskolski M]] |
| - | [[Category: Panjikar, S]] | + | [[Category: Mueller-Dieckmann J]] |
| - | [[Category: Pietrzyk, A J]] | + | [[Category: Panjikar S]] |
| - | [[Category: Beta-trefoil]]
| + | [[Category: Pietrzyk AJ]] |
| - | [[Category: Unknown function]]
| + | |
| - | [[Category: Vhs domain]]
| + | |
| Structural highlights
4efp is a 2 chain structure with sequence from Bombyx mori. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.33Å |
| Ligands: | , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
E5EVW2_BOMMO
Publication Abstract from PubMed
Three crystal structures of a lipoprotein (Bmlp7) of unknown function, a member of the 30 kDa lipoprotein family from mulberry silkworm (Bombyx mori L.) haemolymph, have been determined. The 1.33 A resolution structure is an excellent example of how a precise crystallographic study can contribute to protein identification. The correct sequence of this haemolymph-isolated protein was assigned thanks to superb-quality electron-density maps. Two unexpected cadmium cations were found in this crystal structure [Bmlp7-I(Cd)] and their presence may be connected to a detoxification mechanism in this insect. For a comparison of the metal-binding sites, the crystal structure of a platinum complex (Bmlp7-Pt) was also solved at 1.94 A resolution. The third (2.50 A resolution) structure, of the native protein harvested in a different season (Bmlp7-II), corresponds to a different polymorph with an altered pattern of intermolecular interactions and with a total absence of cadmium ions and highlights the possible involvement of Bmlp7 in the response to environmental pollution. The N-terminal domain of Bmlp7 has a fold resembling a clockwise spiral created by six helices and can be classified as a VHS domain. The C-terminal domain is folded as a beta-trefoil. The biological function of Bmlp7 is unknown, but its structural homology to sugar-binding proteins suggests that, in analogy to other 30 kDa haemolymph lipoproteins, it could play a role as an anti-apoptotic factor or function in the immune response of the insect to fungal infections.
High-resolution structure of Bombyx mori lipoprotein 7: crystallographic determination of the identity of the protein and its potential role in detoxification.,Pietrzyk AJ, Panjikar S, Bujacz A, Mueller-Dieckmann J, Lochynska M, Jaskolski M, Bujacz G Acta Crystallogr D Biol Crystallogr. 2012 Sep;68(Pt 9):1140-51. doi:, 10.1107/S0907444912021555. Epub 2012 Aug 18. PMID:22948915[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pietrzyk AJ, Panjikar S, Bujacz A, Mueller-Dieckmann J, Lochynska M, Jaskolski M, Bujacz G. High-resolution structure of Bombyx mori lipoprotein 7: crystallographic determination of the identity of the protein and its potential role in detoxification. Acta Crystallogr D Biol Crystallogr. 2012 Sep;68(Pt 9):1140-51. doi:, 10.1107/S0907444912021555. Epub 2012 Aug 18. PMID:22948915 doi:http://dx.doi.org/10.1107/S0907444912021555
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