6t44: Difference between revisions
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<StructureSection load='6t44' size='340' side='right'caption='[[6t44]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='6t44' size='340' side='right'caption='[[6t44]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6t44]] is a 2 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5eed 5eed]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T44 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6t44]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5eed 5eed]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T44 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DE1:DECAN-1-OL'>DE1</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]] 2Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DE1:DECAN-1-OL'>DE1</scene></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=6t44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t44 OCA], [https://pdbe.org/6t44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t44 RCSB], [https://www.ebi.ac.uk/pdbsum/6t44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t44 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/LACB_SHEEP LACB_SHEEP] Lactoglobulin is the primary component of whey, it binds retinol and is probably involved in the transport of that molecule. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ovine betaâlactoglobulin was characterized by spectroscopic (CD), calorimetric (ITC) and X-ray structural studies. The structure of ovine betaâlactoglobulin complex with decanol showed that tight packing of molecules in the crystalline phase enforces a distortion of protein flexible loops resulting in the formation of an asymmetric dimer. The loops surrounding beta-barrel in ovine lactoglobulin possessed the same conformational flexibility as observed previously in other lactoglobulins and the change of their conformation regulates the access to the binding pocket. The structure of asymmetric dimer revealed a new region in beta-barrel where ligand polar group can be located. These findings indicated protein adaptability to ligand dimensions and inter- and intramolecular interactions in the crystalline phase. Calorimetric and crystallographic studies provided the experimental evidence that ovine lactoglobulin is able to bind aliphatic ligands. Thermodynamic parameters of sodium dodecyl sulfate binding determined by ITC at pH 7.5 had Ka, DeltaH, TDeltaS and DeltaG values similar to those observed for bovine and caprine protein indicating the same mechanism of ligand binding. | |||
Conformational flexibility and ligand binding properties of ovine beta-lactoglobulin.,Loch J, Bonarek P, Lewinski K Acta Biochim Pol. 2019 Dec 27;66(4):577-584. doi: 10.18388/abp.2019_2883. PMID:31880900<ref>PMID:31880900</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6t44" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Ovis aries]] | ||
[[Category: | [[Category: Kopec M]] | ||
[[Category: | [[Category: Lewinski K]] | ||
[[Category: | [[Category: Loch JI]] | ||
Latest revision as of 15:54, 24 January 2024
Ovine lactoglobulin complex with decanolOvine lactoglobulin complex with decanol
Structural highlights
FunctionLACB_SHEEP Lactoglobulin is the primary component of whey, it binds retinol and is probably involved in the transport of that molecule. Publication Abstract from PubMedOvine betaâlactoglobulin was characterized by spectroscopic (CD), calorimetric (ITC) and X-ray structural studies. The structure of ovine betaâlactoglobulin complex with decanol showed that tight packing of molecules in the crystalline phase enforces a distortion of protein flexible loops resulting in the formation of an asymmetric dimer. The loops surrounding beta-barrel in ovine lactoglobulin possessed the same conformational flexibility as observed previously in other lactoglobulins and the change of their conformation regulates the access to the binding pocket. The structure of asymmetric dimer revealed a new region in beta-barrel where ligand polar group can be located. These findings indicated protein adaptability to ligand dimensions and inter- and intramolecular interactions in the crystalline phase. Calorimetric and crystallographic studies provided the experimental evidence that ovine lactoglobulin is able to bind aliphatic ligands. Thermodynamic parameters of sodium dodecyl sulfate binding determined by ITC at pH 7.5 had Ka, DeltaH, TDeltaS and DeltaG values similar to those observed for bovine and caprine protein indicating the same mechanism of ligand binding. Conformational flexibility and ligand binding properties of ovine beta-lactoglobulin.,Loch J, Bonarek P, Lewinski K Acta Biochim Pol. 2019 Dec 27;66(4):577-584. doi: 10.18388/abp.2019_2883. PMID:31880900[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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