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1fre
From Proteopedia
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==Overview== | ==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, ... | + | 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== | ==About this Structure== | ||
| - | 1FRE is a | + | 1FRE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: ZN1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FRE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zinc-binding protein]] | [[Category: zinc-binding protein]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:37:17 2007'' |
Revision as of 12:31, 5 November 2007
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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. Structure known Active Site: ZN1. 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
Page seeded by OCA on Mon Nov 5 14:37:17 2007
