3B0K

Crystal structure of alpha-lactalbumin

Summary for 3B0K

• Entry DOI: 10.2210/pdb3b0k/pdb
• Related: 3B0I 3B0O
• Descriptor: Alpha-lactalbumin, CALCIUM ION (3 entities in total)
• Functional Keywords: calcium binding protein, glycoprotein, metal binding protein
• Biological source: Capra hircus (Goat)
• Cellular location: Secreted: P00712
• Total number of polymer chains: 2
• Total formula weight: 28506.44

Authors

Makabe, K. (deposition date: 2011-06-10, release date: 2012-06-13, Last modification date: 2024-11-20)

Primary citation

Makabe, K.,Nakamura, T.,Kuwajima, K.
Structural insights into the stability perturbations induced by N-terminal variation in human and goat alpha-lactalbumin
Protein Eng.Des.Sel., 26:165-170, 2013

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.

PubMed: 23155056
DOI: 10.1093/protein/gzs093

Experimental method

X-RAY DIFFRACTION (1.6 Å)