3b0i | pdb_00003b0i
Crystal structure of recombinant human alpha lactalbumin
Structural highlights
FunctionLALBA_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. 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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