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| | ==NMR structure of the C-terminal domain of EW29== | | ==NMR structure of the C-terminal domain of EW29== |
| - | <StructureSection load='2rst' size='340' side='right'caption='[[2rst]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2rst' size='340' side='right'caption='[[2rst]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2rst]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Common_earthworm Common earthworm]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RST OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2RST FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2rst]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lumbricus_terrestris Lumbricus terrestris]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RST OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RST FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2rst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rst OCA], [http://pdbe.org/2rst PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rst RCSB], [http://www.ebi.ac.uk/pdbsum/2rst PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rst ProSAT]</span></td></tr> | + | </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=2rst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rst OCA], [https://pdbe.org/2rst PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rst RCSB], [https://www.ebi.ac.uk/pdbsum/2rst PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rst 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: Large Structures]] |
| - | [[Category: Hemmi, H]] | + | [[Category: Lumbricus terrestris]] |
| - | [[Category: R-type lectin]] | + | [[Category: Hemmi H]] |
| - | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
Function
O96048_LUMTE
Publication Abstract from PubMed
The C-terminal domain (Ch; C-half) of the R-type earthworm 29-kDa lectin (EW29), isolated from the earthworm Lumbricus terrestris, has two sugar-binding sites, in subdomains alpha and gamma, and the protein uses the two sugar-binding sites for its function as a single domain-type haemagglutinin. Our previous NMR titration experiments showed that the alpha sugar-binding site is a high-affinity site and the gamma sugar-binding site is a low-affinity site. However, it remains unclear why the alpha sugar-binding site of EW29Ch binds to lactose much more strongly because the crystal structure of lactose-bound EW29Ch showed that the interaction between the alpha sugar-binding site and lactose was almost same as that between the gamma sugar-binding site and lactose. In the present study, we have determined the NMR structure of EW29Ch in the sugar-free state and performed (15)N relaxation experiments for EW29Ch in both the sugar-free state and the lactose-bound states. The conformation of EW29Ch in the sugar-free state was similar to that of EW29Ch in complex with lactose. Conformational changes upon binding of lactose were observed only for the alpha sugar-binding site. By contrast, the (15)N relaxation experiments revealed a conformational exchange at the alpha sugar-binding site in the sugar-free state, which was suppressed in the lactose-bound state. The conformational exchange phenomenon observed for the alpha sugar-binding site was not observed for the gamma sugar-binding site. Differences in the conformational change and the backbone dynamics between subdomains alpha and gamma may be associated with the difference of the sugar-binding modes between the two sugar-binding sites. DATABASE: Structural data for the NMR structure of EW29Ch in the sugar-free state have been deposited in the Protein Data Bank database under accession number 2RST.
NMR structure and dynamics of the C-terminal domain of R-type lectin from the earthworm Lumbricus terrestris.,Hemmi H, Kuno A, Hirabayashi J FEBS J. 2013 Jan;280(1):70-82. doi: 10.1111/febs.12050. Epub 2012 Nov 23. PMID:23122331[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hemmi H, Kuno A, Hirabayashi J. NMR structure and dynamics of the C-terminal domain of R-type lectin from the earthworm Lumbricus terrestris. FEBS J. 2013 Jan;280(1):70-82. doi: 10.1111/febs.12050. Epub 2012 Nov 23. PMID:23122331 doi:http://dx.doi.org/10.1111/febs.12050
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