4nlj: Difference between revisions
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==Crystal structure of sheep beta-lactoglobulin (space group P1)== | ==Crystal structure of sheep beta-lactoglobulin (space group P1)== | ||
<StructureSection load='4nlj' size='340' side='right' caption='[[4nlj]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='4nlj' size='340' side='right'caption='[[4nlj]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4nlj]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4nlj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NLJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NLJ FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4nlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nlj OCA], [https://pdbe.org/4nlj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nlj RCSB], [https://www.ebi.ac.uk/pdbsum/4nlj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nlj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 15: | Line 18: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4nlj" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Ovis aries]] | [[Category: Ovis aries]] | ||
[[Category: Kopec | [[Category: Kopec M]] | ||
[[Category: Lewinski | [[Category: Lewinski K]] | ||
[[Category: Loch | [[Category: Loch JI]] | ||
[[Category: Molenda | [[Category: Molenda M]] | ||
[[Category: Swiatek | [[Category: Swiatek S]] | ||
Latest revision as of 17:48, 8 November 2023
Crystal structure of sheep beta-lactoglobulin (space group P1)Crystal structure of sheep beta-lactoglobulin (space group P1)
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 beta-lactoglobulin has been isolated from whey fraction of sheep milk and crystallized. The high-resolution structures of two crystal forms (triclinic and trigonal) obtained at pH 7.0 have been determined revealing that ovine protein, similarly to its bovine analog, is dimeric. Access to the binding site located in the eight-stranded antiparallel beta-barrel in both structures is blocked by the EF loop that has been found in closed conformation. Similarly to bovine lactoglobulin (BLG), conformation of the EF loop is stabilized by hydrogen bond between Glu89 and Ser116 indicating that Tanford transition might occur with the same mechanism. The substitution at six positions in relation to the most abundant isoform B of BLG also affects the distribution of electrostatic potentials and the total charge. (c) 2014 Wiley Periodicals, Inc. Biopolymers 101: 886-894, 2014. Structure of two crystal forms of sheep beta-lactoglobulin with EF-loop in closed conformation.,Loch JI, Molenda M, Kopec M, Swiatek S, Lewinski K Biopolymers. 2014 Aug;101(8):886-94. doi: 10.1002/bip.22471. PMID:25098178[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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