α-lactalbumin possesses a distinct zinc binding site

Jingshan Ren, David I. Stuart, K. Ravi Acharya

Research output: Contribution to journalArticle

Abstract

It has been proposed that the binding of Zn2+ to α-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 α-lactalbumin-Zn2+ complex at 1.7-Å 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 α-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 SO42- ion bound at the interface between three molecules.

Original languageEnglish
Pages (from-to)19292-19298
Number of pages7
JournalJournal of Biological Chemistry
Volume268
Issue number26
Publication statusPublished - 15 Sep 1993

ASJC Scopus subject areas

  • Biochemistry

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