|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='2y9g' size='340' side='right'caption='[[2y9g]], [[Resolution|resolution]] 1.67Å' scene=''> | | <StructureSection load='2y9g' size='340' side='right'caption='[[2y9g]], [[Resolution|resolution]] 1.67Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2y9g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Boletus_sulphureus_bull.,_1789 Boletus sulphureus bull., 1789]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y9G OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2Y9G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2y9g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Laetiporus_sulphureus Laetiporus sulphureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y9G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y9G 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=LAT:BETA-LACTOSE'>LAT</scene>, <scene name='pdbligand=LBT:ALPHA-LACTOSE'>LBT</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]] 1.67Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2y9f|2y9f]], [[1w3a|1w3a]], [[1w3f|1w3f]], [[1w3g|1w3g]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRD_900004:beta-lactose'>PRD_900004</scene>, <scene name='pdbligand=PRD_900008:alpha-lactose'>PRD_900008</scene></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=2y9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y9g OCA], [http://pdbe.org/2y9g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2y9g RCSB], [http://www.ebi.ac.uk/pdbsum/2y9g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2y9g 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=2y9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y9g OCA], [https://pdbe.org/2y9g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y9g RCSB], [https://www.ebi.ac.uk/pdbsum/2y9g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y9g ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q7Z8V1_9APHY Q7Z8V1_9APHY] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Boletus sulphureus bull., 1789]] | + | [[Category: Laetiporus sulphureus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Acebron, I]] | + | [[Category: Acebron I]] |
| - | [[Category: Angulo, I]] | + | [[Category: Angulo I]] |
| - | [[Category: Garcia, P]] | + | [[Category: Garcia P]] |
| - | [[Category: Goldstein, I J]] | + | [[Category: Goldstein IJ]] |
| - | [[Category: Mancheno, J M]] | + | [[Category: Mancheno JM]] |
| - | [[Category: Menendez, M]] | + | [[Category: Menendez M]] |
| - | [[Category: Munoz, R]] | + | [[Category: Munoz R]] |
| - | [[Category: Perez-Agote, B]] | + | [[Category: Perez-Agote B]] |
| - | [[Category: Rivas, B de las]]
| + | [[Category: Rodriguez JI]] |
| - | [[Category: Rodriguez, J I]] | + | [[Category: Tateno H]] |
| - | [[Category: Tateno, H]] | + | [[Category: De las Rivas B]] |
| - | [[Category: Sugar binding protein]] | + | |
| Structural highlights
2y9g is a 1 chain structure with sequence from Laetiporus sulphureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.67Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q7Z8V1_9APHY
Publication Abstract from PubMed
In this work, we analyzed at high resolution the sugar-binding mode of the recombinant N-terminal ricin-B domain of the hemolytic protein LSLa (LSL(150)) from the mushroom Laetiporus sulphureus and also provide functional in vitro evidence suggesting that, together with its putative receptor-binding role, this module may also increase the solubility of its membrane pore-forming partner. We first demonstrate that recombinant LSL(150) behaves as an autonomous folding unit and an active lectin. We have determined its crystal structure at 1.47 A resolution and also that of the [LSL(150):(lactose)beta, gamma)] binary complex at 1.67 A resolution. This complex reveals two lactose molecules bound to the beta and gamma sites of LSL(150), respectively. Isothermal titration calorimetry indicates that LSL(150) binds two lactoses in solution with highly different affinities. Also, we test the working hypothesis that LSL(150) exhibits in vivo properties typical of solubility tags. With this aim, we have fused an engineered version of LSL(150) (LSL(t)) to the N-terminal end of various recombinant proteins. All the designed LSL(150)-tagged fusion proteins were successfully produced at high yield, and furthermore, the target proteins were purified by a straightforward affinity procedure on agarose-based matrices due to the excellent properties of LSL(150) as an affinity tag. An optimized protocol for target protein purification was devised, which involved removal of the LSL(150) tag through in-column cleavage of the fusion proteins with His(6)-tagged TEV endoprotease. These results permitted to set up a novel, lectin-based system for production and purification of recombinant proteins in E. coli cells with attractive biotechnological applications.
High-resolution structural insights on the sugar-recognition and fusion tag properties of a versatile beta-trefoil lectin domain from the mushroom Laetiporus sulphureus.,Angulo I, Acebron I, de las Rivas B, Munoz R, Rodriguez-Crespo I, Menendez M, Garcia P, Tateno H, Goldstein IJ, Perez-Agote B, Mancheno JM Glycobiology. 2011 Oct;21(10):1349-61. Epub 2011 Jun 1. PMID:21632870[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Angulo I, Acebron I, de las Rivas B, Munoz R, Rodriguez-Crespo I, Menendez M, Garcia P, Tateno H, Goldstein IJ, Perez-Agote B, Mancheno JM. High-resolution structural insights on the sugar-recognition and fusion tag properties of a versatile beta-trefoil lectin domain from the mushroom Laetiporus sulphureus. Glycobiology. 2011 Oct;21(10):1349-61. Epub 2011 Jun 1. PMID:21632870 doi:10.1093/glycob/cwr074
|
