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2dry

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(New page: 200px<br /><applet load="2dry" size="350" color="white" frame="true" align="right" spinBox="true" caption="2dry, resolution 1.80&Aring;" /> '''Crystal structure of...)
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[[Image:2dry.jpg|left|200px]]<br /><applet load="2dry" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2dry, resolution 1.80&Aring;" />
 
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'''Crystal structure of the earthworm lectin C-terminal domain mutant'''<br />
 
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==Overview==
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==Crystal structure of the earthworm lectin C-terminal domain mutant==
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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.
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<StructureSection load='2dry' size='340' side='right'caption='[[2dry]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<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>
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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=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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/O96048_LUMTE O96048_LUMTE]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:17234683</ref>
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2DRY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lumbricus_terrestris Lumbricus terrestris] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=PGE:'>PGE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DRY OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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 (Tokyo). 2007 Jan 18;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17234683 17234683]
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</div>
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[[Category: Lumbricus terrestris]]
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<div class="pdbe-citations 2dry" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Fujimoto, Z.]]
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[[Category: Suzuki, R.]]
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[[Category: PGE]]
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[[Category: SO4]]
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[[Category: beta-trefoil fold]]
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[[Category: earthworm lumbricus terrestris]]
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[[Category: galactose]]
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[[Category: in vitro evolution]]
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[[Category: sialic acid]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:10:43 2008''
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==See Also==
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*[[Galactose-binding lectin|Galactose-binding lectin]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Lumbricus terrestris]]
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[[Category: Fujimoto Z]]
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[[Category: Suzuki R]]

Current revision

Crystal structure of the earthworm lectin C-terminal domain mutant

PDB ID 2dry

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