3mgw
From Proteopedia
(Difference between revisions)
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| - | + | ==Thermodynamics and structure of a salmon cold-active goose-type lysozyme== | |
| - | + | <StructureSection load='3mgw' size='340' side='right' caption='[[3mgw]], [[Resolution|resolution]] 1.75Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3mgw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atlantic_salmon Atlantic salmon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MGW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MGW FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lysG, LYG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8030 Atlantic salmon])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </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=3mgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mgw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mgw RCSB], [http://www.ebi.ac.uk/pdbsum/3mgw PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mg/3mgw_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Atlantic salmon goose-type lysozyme (SalG) was previously shown to display features of cold-adaptation as well as renaturation following heat treatment. In this study differential scanning calorimetry (DSC) was carried out to investigate unfolding and potential refolding, while X-ray crystallography was used to study structural factors contributing to the temperature-related characteristics. The recombinant SalG has a melting temperature (T(m)) of 36.8 degrees C under thermal denaturation conditions and regains activity after returning to permissive (low) temperature. Furthermore, refolding is dramatically reduced in solutions with high SalG concentrations, coupled with significant protein precipitation. The structural features of SalG closely resemble those of other g-type lysozymes. However, the N-terminal region of SalG is less anchored to the rest of the molecule due to the absence of disulphide bonds, thus, contributing significantly to the low T(m) of SalG. The absence of disulphide bonds and the distribution of salt bridges may at the same time ease refolding leading to renaturation. | ||
| - | + | Thermodynamics and structure of a salmon cold active goose-type lysozyme.,Kyomuhendo P, Myrnes B, Brandsdal BO, Smalas AO, Nilsen IW, Helland R Comp Biochem Physiol B Biochem Mol Biol. 2010 Aug;156(4):254-63. Epub 2010, Apr 14. PMID:20398783<ref>PMID:20398783</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
==See Also== | ==See Also== | ||
| - | *[[ | + | *[[Lysozyme 3D structures|Lysozyme 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Atlantic salmon]] | [[Category: Atlantic salmon]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
| - | [[Category: Brandsdal, B O | + | [[Category: Brandsdal, B O]] |
| - | [[Category: Helland, R | + | [[Category: Helland, R]] |
| - | [[Category: Kyomuhendo, P | + | [[Category: Kyomuhendo, P]] |
| - | [[Category: Myrnes, B | + | [[Category: Myrnes, B]] |
| - | [[Category: Nilsen, I W | + | [[Category: Nilsen, I W]] |
| - | [[Category: Smalas, A O | + | [[Category: Smalas, A O]] |
[[Category: Differential scanning calorimetry]] | [[Category: Differential scanning calorimetry]] | ||
[[Category: Goose-type]] | [[Category: Goose-type]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Innate immunity]] | [[Category: Innate immunity]] | ||
| - | [[Category: Lysozyme]] | ||
[[Category: Refolding]] | [[Category: Refolding]] | ||
[[Category: Salmon]] | [[Category: Salmon]] | ||
[[Category: Thermal tolerance]] | [[Category: Thermal tolerance]] | ||
Revision as of 17:19, 21 December 2014
Thermodynamics and structure of a salmon cold-active goose-type lysozyme
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