1HML

ALPHA_LACTALBUMIN POSSESSES A DISTINCT ZINC BINDING SITE

Summary for 1HML

• Entry DOI: 10.2210/pdb1hml/pdb
• Descriptor: ALPHA-LACTALBUMIN, CALCIUM ION, ZINC ION, ... (5 entities in total)
• Functional Keywords: calcium-binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 16442.41

Authors

Ren, J.,Stuart, D.I.,Acharya, K.R. (deposition date: 1994-09-29, release date: 1995-01-26, Last modification date: 2024-11-20)

Primary citation

Ren, J.,Stuart, D.I.,Acharya, K.R.
Alpha-lactalbumin possesses a distinct zinc binding site.
J.Biol.Chem., 268:19292-19298, 1993

PubMed Abstract: It has been proposed that the binding of Zn2+ to alpha-lactalbumin switches the conformation to one akin to a state intermediate in the folding of the protein. However, the high resolution x-ray crystal structure of human alpha-lactalbumin-Zn2+ complex at 1.7-A resolution (pH 7.6) does not reveal any significant change in conformation from the native state. The Zn2+ ion binds specifically in the "cleft" of alpha-lactalbumin (the region which forms the active site of the homologous protein lysozyme). This may suggest a possible role for Zn2+ binding in lactose synthase complex. The coordination of the Zn2+ ion involves a symmetry-related molecule in the crystal, the crystal contacts being stabilized by a SO4(2-) ion bound at the interface between three molecules.

PubMed: 8366079

Experimental method

X-RAY DIFFRACTION (1.7 Å)