1hml
From Proteopedia
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ALPHA_LACTALBUMIN POSSESSES A DISTINCT ZINC BINDING SITE
Overview
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.
About this Structure
1HML is a Single protein structure of sequence from Homo sapiens with CA, ZN and SO4 as ligands. Active as Lactose synthase, with EC number 2.4.1.22 Full crystallographic information is available from OCA.
Reference
Alpha-lactalbumin possesses a distinct zinc binding site., Ren J, Stuart DI, Acharya KR, J Biol Chem. 1993 Sep 15;268(26):19292-8. PMID:8366079
Page seeded by OCA on Mon Nov 12 17:20:12 2007
Categories: Homo sapiens | Lactose synthase | Single protein | Acharya, K.R. | Ren, J. | Stuart, D.I. | CA | SO4 | ZN | Calcium-binding protein
