1fre
From Proteopedia
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XNF7 BBOX, DEVELOPMENTAL PROTEIN, PH 7.5, 30 C, WITH ZINC, NMR, 1 STRUCTURE
Overview
Xenopus nuclear factor XNF7, a maternally expressed protein, functions in, patterning of the embryo. XNF7 contains a number of defined protein, domains implicated in the regulation of some developmental processes., Among these is a tripartite motif comprising a zinc-binding RING finger, and B-box domain next to a predicted alpha-helical coiled-coil domain., Interestingly, this motif is found in a variety of protein including, several proto-oncoproteins. Here we describe the solution structure of the, XNF7 B-box zinc-binding domain determined at physiological pH by 1H NMR, methods. The B-box structure represents the first three-dimensional, structure of this new motif and comprises a monomer have two beta-strands, two helical turns and three extended loop regions packed in a novel, topology. The r.m.s. deviation for the best 18 structures is 1.15 A for, backbone atoms and 1.94 A for all atoms. Structure calculations and, biochemical data shows one zinc atom ligated in a Cys2-His2 tetrahedral, arrangement. We have used mutant peptides to determine the metal ligation, scheme which surprisingly shows that not all of the seven conserved, cysteines/histidines in the B-box motif are involved in metal ligation., The B-box structure is not similar in tertiary fold to any other known, zinc-binding motif.
About this Structure
1FRE is a Single protein structure of sequence from Xenopus laevis with ZN as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Novel topology of a zinc-binding domain from a protein involved in regulating early Xenopus development., Borden KL, Lally JM, Martin SR, O'Reilly NJ, Etkin LD, Freemont PS, EMBO J. 1995 Dec 1;14(23):5947-56. PMID:8846787
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