View source for 4omw


==Crystal structure of goat beta-lactoglobulin (orthorhombic form)==
<StructureSection load='4omw' size='340' side='right'caption='[[4omw]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4omw]] is a 4 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=4OMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OMW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TE4:TETRACAINE'>TE4</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=4omw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4omw OCA], [https://pdbe.org/4omw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4omw RCSB], [https://www.ebi.ac.uk/pdbsum/4omw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4omw ProSAT]</span></td></tr>
</table>
== 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;">
== Publication Abstract from PubMed ==
Goat 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<ref>PMID:25450833</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4omw" style="background-color:#fffaf0;"></div>

==See Also==
*[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Capra hircus]]
[[Category: Large Structures]]
[[Category: Czub M]]
[[Category: Lewinski K]]
[[Category: Loch JI]]
[[Category: Ludwikowska M]]
[[Category: Swiatek S]]