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| | ==Crystal structure of the earthworm lectin C-terminal domain mutant== | | ==Crystal structure of the earthworm lectin C-terminal domain mutant== |
| - | <StructureSection load='2dry' size='340' side='right' caption='[[2dry]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='2dry' size='340' side='right'caption='[[2dry]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2dry]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Common_earthworm Common earthworm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DRY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DRY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2dry]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lumbricus_terrestris Lumbricus terrestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DRY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DRY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ao3|2ao3]], [[2d12|2d12]], [[2drz|2drz]], [[2ds0|2ds0]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2dry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dry OCA], [http://pdbe.org/2dry PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dry RCSB], [http://www.ebi.ac.uk/pdbsum/2dry PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2dry 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=2dry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dry OCA], [https://pdbe.org/2dry PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dry RCSB], [https://www.ebi.ac.uk/pdbsum/2dry PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dry ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O96048_LUMTE O96048_LUMTE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Common earthworm]] | + | [[Category: Large Structures]] |
| - | [[Category: Fujimoto, Z]] | + | [[Category: Lumbricus terrestris]] |
| - | [[Category: Suzuki, R]] | + | [[Category: Fujimoto Z]] |
| - | [[Category: Beta-trefoil fold]] | + | [[Category: Suzuki R]] |
| - | [[Category: Earthworm lumbricus terrestri]]
| + | |
| - | [[Category: Galactose]]
| + | |
| - | [[Category: In vitro evolution]]
| + | |
| - | [[Category: Sialic acid]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
Function
O96048_LUMTE
Publication Abstract from PubMed
Sialic acid (Sia) is a typical terminal sugar, which modifies various types of glycoconjugates commonly found in higher animals. Its regulatory roles in diverse biological phenomena are frequently triggered by interaction with Sia-binding lectins. When using natural Sia-binding lectins as probes, however, there have been practical problems concerning their repertoire and availability. Here, we show a rational creation of a Sia-binding lectin based on the strategy 'natural evolution-mimicry', where Sia-binding lectins are engineered by error-prone PCR from a Gal-binding lectin used as a scaffold protein. After selection with fetuin-agarose using a recently reinforced ribosome display system, one of the evolved mutants SRC showed substantial affinity for alpha2-6Sia, which the parental Gal-binding lectin EW29Ch lacked. SRC was found to have additional practical advantages in productivity and in preservation of affinity for Gal. Thus, the developed novel Sia-recognition protein will contribute as useful tools to sialoglycomics.
Tailoring a novel sialic acid-binding lectin from a ricin-B chain-like galactose-binding protein by natural evolution-mimicry.,Yabe R, Suzuki R, Kuno A, Fujimoto Z, Jigami Y, Hirabayashi J J Biochem. 2007 Mar;141(3):389-99. Epub 2007 Jan 18. PMID:17234683[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yabe R, Suzuki R, Kuno A, Fujimoto Z, Jigami Y, Hirabayashi J. Tailoring a novel sialic acid-binding lectin from a ricin-B chain-like galactose-binding protein by natural evolution-mimicry. J Biochem. 2007 Mar;141(3):389-99. Epub 2007 Jan 18. PMID:17234683 doi:10.1093/jb/mvm043
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