3b0o
From Proteopedia
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| - | [[Image:3b0o.jpg|left|200px]] | ||
| - | + | ==Crystal structure of alpha-lactalbumin== | |
| - | + | <StructureSection load='3b0o' size='340' side='right'caption='[[3b0o]], [[Resolution|resolution]] 1.61Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3b0o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B0O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B0O 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]] 1.61Å</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=3b0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b0o OCA], [https://pdbe.org/3b0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b0o RCSB], [https://www.ebi.ac.uk/pdbsum/3b0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b0o ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/LALBA_HUMAN LALBA_HUMAN] 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 3b0o" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | [[ | + | *[[Alpha-lactalbumin 3D structures|Alpha-lactalbumin 3D structures]] |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Kuwajima K]] |
| - | [[Category: | + | [[Category: Makabe K]] |
| - | + | ||
Current revision
Crystal structure of alpha-lactalbumin
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