4omx: Difference between revisions
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<StructureSection load='4omx' size='340' side='right'caption='[[4omx]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='4omx' size='340' side='right'caption='[[4omx]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4omx]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4omx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Capra_hircus Capra hircus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OMX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OMX FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ARF:FORMAMIDE'>ARF</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=URE:UREA'>URE</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ARF:FORMAMIDE'>ARF</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=URE:UREA'>URE</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=4omx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4omx OCA], [https://pdbe.org/4omx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4omx RCSB], [https://www.ebi.ac.uk/pdbsum/4omx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4omx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/LACB_CAPHI LACB_CAPHI] 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 == | ||
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[[Category: Capra hircus]] | [[Category: Capra hircus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Czub | [[Category: Czub M]] | ||
[[Category: Lewinski | [[Category: Lewinski K]] | ||
[[Category: Loch | [[Category: Loch JI]] | ||
[[Category: Ludwikowska | [[Category: Ludwikowska M]] | ||
[[Category: Swiatek | [[Category: Swiatek S]] | ||
Latest revision as of 20:16, 20 September 2023
Crystal structure of goat beta-lactoglobulin (trigonal form)Crystal structure of goat beta-lactoglobulin (trigonal form)
Structural highlights
FunctionLACB_CAPHI Primary component of whey, it binds retinol and is probably involved in the transport of that molecule. Publication Abstract from PubMedGoat beta-lactoglobulin (GLG), lipocalin protein sharing high sequence similarity to bovine beta-lactoglobulin (BLG), has been structurally and thermodynamically characterized. Two crystal forms of GLG have been obtained, trigonal (P3121) and orthorhombic (P21212), with unique molecular packing, not observed previously for BLG. In the trigonal structure, GLG molecules have EF-loop in closed conformation while in the orthorhombic structure, for the first time, symmetric and asymmetric dimers of beta-lactoglobulin are observed simultaneously. It indicates that the opening or closing EF-loop does not occur in both subunits at the same time but might be sequential and cooperative. Comparison of GLG and BLG structures revealed presence of various conformers of EF and GH. ITC studies showed that at pH 7.5 GLG binds sodium dodecyl sulfate with Gibbs energy similar to BLG, however, with different contribution from enthalpic and entropic component. At pH 7.5 GLG forms dimers with dimerization constant Ka=34.28x10(3)M(-1), significantly higher than observed for BLG. Similar mechanism of conformational changes and ligand binding indicates that GLG and BLG may play analogous biological role. Conformational variability of goat beta-lactoglobulin: Crystallographic and thermodynamic studies.,Loch JI, Bonarek P, Polit A, Swiatek S, Czub M, Ludwikowska M, Lewinski K Int J Biol Macromol. 2015 Jan;72:1283-91. doi: 10.1016/j.ijbiomac.2014.10.031., Epub 2014 Oct 24. PMID:25450833[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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