3B0K

Structural insights into the stability perturbations induced by N-terminal variation in human and goat alpha-lactalbumin

(2013) Protein Eng Des Sel 26: 165-170

• PubMed: 23155056 Search on PubMed
• DOI: https://doi.org/10.1093/protein/gzs093
• Primary Citation of Related Structures:  
  3B0I, 3B0K, 3B0O


• PubMed Abstract: 
  

  Addition of an extra methionine at the N-terminus by recombinant expression of α-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 α-lactalbumin. Here, we thus determined the crystal structures of the residue 1-deletion variants of recombinant human and goat α-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 α-lactalbumin.

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Organizational Affiliation: 

Okazaki Institute for Integrative Bioscience and Institute for Molecular Science, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki 444-8787, Japan. makabe@yz.yamagata-u.ac.jp