1FRE

XNF7 BBOX, DEVELOPMENTAL PROTEIN, PH 7.5, 30 C, WITH ZINC, NMR, 1 STRUCTURE

Summary for 1FRE

• Entry DOI: 10.2210/pdb1fre/pdb
• Descriptor: NUCLEAR FACTOR XNF7, ZINC ION (2 entities in total)
• Functional Keywords: zinc-binding protein, xnf7, bbox, development, mid-blastula-transition
• Biological source: Xenopus laevis (African clawed frog)
• Total number of polymer chains: 1
• Total formula weight: 4947.05

Authors

Borden, K.L.B.,Freemont, P.S. (deposition date: 1996-01-31, release date: 1997-02-12, Last modification date: 2024-05-22)

Primary citation

Borden, K.L.,Lally, J.M.,Martin, S.R.,O'Reilly, N.J.,Etkin, L.D.,Freemont, P.S.
Novel topology of a zinc-binding domain from a protein involved in regulating early Xenopus development.
EMBO J., 14:5947-5956, 1995

PubMed Abstract: 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.

PubMed: 8846787

Experimental method

SOLUTION NMR