1HFX

ALPHA-LACTALBUMIN

Summary for 1HFX

• Entry DOI: 10.2210/pdb1hfx/pdb
• Descriptor: ALPHA-LACTALBUMIN, CALCIUM ION (3 entities in total)
• Functional Keywords: lactose synthase component, calcium binding metalloprotein, lactose, glycoprotein
• Biological source: Cavia porcellus (domestic guinea pig)
• Total number of polymer chains: 1
• Total formula weight: 14280.24

Authors

Pike, A.C.W.,Brew, K.,Acharya, K.R. (deposition date: 1996-06-13, release date: 1997-07-07, Last modification date: 2024-11-20)

Primary citation

Pike, A.C.,Brew, K.,Acharya, K.R.
Crystal structures of guinea-pig, goat and bovine alpha-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase.
Structure, 4:691-703, 1996

PubMed Abstract: The regulation of milk lactose biosynthesis is highly dependent on the action of a specifier protein, alpha-lactalbumin (LA). Together with a glycosyltransferase, LA forms the enzyme complex lactose synthase. LA promotes the binding of glucose to the complex and facilitates the biosynthesis of lactose. To gain further insight into the molecular basis of LA function in lactose synthase we have determined the structures of three species variants of LA.

PubMed: 8805552
DOI: 10.1016/S0969-2126(96)00075-5

Experimental method

X-RAY DIFFRACTION (1.9 Å)