3b0k: Difference between revisions
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==Crystal structure of alpha-lactalbumin== | ==Crystal structure of alpha-lactalbumin== | ||
<StructureSection load='3b0k' size='340' side='right' caption='[[3b0k]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='3b0k' size='340' side='right'caption='[[3b0k]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3b0k]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3b0k]] is a 2 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=3B0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B0K 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]] 1.6Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3b0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b0k OCA], [https://pdbe.org/3b0k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b0k RCSB], [https://www.ebi.ac.uk/pdbsum/3b0k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b0k ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/LALBA_CAPHI LALBA_CAPHI] Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 21: | ||
==See Also== | ==See Also== | ||
*[[Alpha-lactalbumin|Alpha-lactalbumin]] | *[[Alpha-lactalbumin 3D structures|Alpha-lactalbumin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Capra hircus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Makabe K]] | ||
Latest revision as of 11:51, 11 October 2023
Crystal structure of alpha-lactalbuminCrystal structure of alpha-lactalbumin
Structural highlights
FunctionLALBA_CAPHI Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins. Publication Abstract from PubMedAddition of an extra methionine at the N-terminus by recombinant expression of alpha-lactalbumin in Escherichia coli significantly destabilizes the protein, and this destabilization has hampered mutational analyses such as the mutational phi-value analysis of the protein. Deletion of residue 1 from the recombinant form recovers the stability in human and goat alpha-lactalbumin. Here, we thus determined the crystal structures of the residue 1-deletion variants of recombinant human and goat alpha-lactalbumin, and compared the structures with those of the authentic and recombinant forms. The results demonstrate the importance of the N-terminal backbone structure and hydrogen-bonding pattern for the stability of alpha-lactalbumin. Structural insights into the stability perturbations induced by N-terminal variation in human and goat alpha-lactalbumin.,Makabe K, Nakamura T, Kuwajima K Protein Eng Des Sel. 2013 Feb;26(2):165-70. doi: 10.1093/protein/gzs093. Epub, 2012 Nov 14. PMID:23155056[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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