5d5g: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Structure of colocasia esculenta agglutinin== | ==Structure of colocasia esculenta agglutinin== | ||
<StructureSection load='5d5g' size='340' side='right' caption='[[5d5g]], [[Resolution|resolution]] 1.74Å' scene=''> | <StructureSection load='5d5g' size='340' side='right'caption='[[5d5g]], [[Resolution|resolution]] 1.74Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<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> | <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> | </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://www.rcsb.org/pdb/explore.do?structureId=5d5g RCSB], [http://www.ebi.ac.uk/pdbsum/5d5g PDBsum]</span></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> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== 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 <--> 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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5d5g" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Agglutinin 3D structures|Agglutinin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Colocasia esculenta]] | [[Category: Colocasia esculenta]] | ||
[[Category: Large Structures]] | |||
[[Category: Biswas, H]] | [[Category: Biswas, H]] | ||
[[Category: Chattopadhyaya, R]] | [[Category: Chattopadhyaya, R]] | ||
