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1fre

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==Overview==
==Overview==
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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.
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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==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
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[[Category: Borden, K.L.B.]]
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[[Category: Borden, K L.B.]]
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[[Category: Freemont, P.S.]]
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[[Category: Freemont, P S.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: bbox]]
[[Category: bbox]]
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[[Category: zinc-binding protein]]
[[Category: zinc-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:40:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:41:52 2008''

Revision as of 10:42, 21 February 2008


1fre

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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 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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