5d5g

<table><tr><td colspan='2'>[[5d5g]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Colocasia_esculenta Colocasia esculenta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D5G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D5G FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5d5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d5g OCA], [http://pdbe.org/5d5g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d5g RCSB], [http://www.ebi.ac.uk/pdbsum/5d5g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d5g ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The major tuber storage protein of Colocasia esculenta, is a monocot mannose-binding, widely used dietary lectin, containing two polypeptides of 12.0 and 12.4 kDa. By both gel filtration and dynamic light scattering at pH 7.2, the lectin has a alpha2beta2 form of apparent molecular mass of 48.2 kDa and a hydrodynamic radius of 6.1 +/- .2 nm; however, at pH 3, it migrates as alphabeta and has a reduced hydrodynamic radius of 4.6 +/- .3 nm. Our circular dichroism spectroscopy studies show that the lectin retains approximately 100% of its secondary structure between pH 2-8, going down to ~90% for extreme acidic/alkaline conditions. The fluorescence emission maxima of 346 to 350 nm for pH 4 to 10 show that the tryptophan residues are relatively exposed. The unfolding is a simple two-state process, N4 &lt;--&gt; 4U, as seen in our denaturation scan profiles. These denaturation profiles, monitored separately by fluorescence, far-UV CD, and near-UV CD, are completely super imposable. Analyses of these profiles provide an estimate of several thermodynamic parameters at each guanidinium chloride concentration, including the melting temperature Tg, which is 346.9 K in 0 M, but lowers to 321.8 K in 3.6 M. Dimeric and tetrameric interfaces observed in the crystal structure for the same protein are used to rationalize solution data in some detail.

 

Thermal and chemical denaturation of Colocasia esculenta tuber agglutinin from alpha2beta2 to unfolded state.,Biswas H, Chattopadhyaya R J Biomol Struct Dyn. 2018 Jun;36(8):2179-2193. doi:, 10.1080/07391102.2017.1345327. Epub 2017 Sep 8. PMID:28633569<ref>PMID:28633569</ref>

 

== References ==

<references/>

[[Category: Biswas, H]]

[[Category: Chattopadhyaya, R]]

[[Category: Sugar binding protein]]