3b0k: Difference between revisions
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< | ==Crystal structure of alpha-lactalbumin== | ||
<StructureSection load='3b0k' size='340' side='right'caption='[[3b0k]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<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='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='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> | |||
</table> | |||
== 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;"> | |||
== Publication Abstract from PubMed == | |||
Addition 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<ref>PMID:23155056</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3b0k" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Alpha-lactalbumin 3D structures|Alpha-lactalbumin 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Capra hircus]] | [[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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