3b0k: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3b0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b0k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3b0k RCSB], [http://www.ebi.ac.uk/pdbsum/3b0k PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3b0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b0k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3b0k RCSB], [http://www.ebi.ac.uk/pdbsum/3b0k PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://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. | |||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 10:10, 25 December 2014
Crystal structure of alpha-lactalbuminCrystal structure of alpha-lactalbumin
Structural highlights
Function[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. 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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