This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1fre

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1fre.gif|left|200px]]<br /><applet load="1fre" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1fre.gif|left|200px]]
-
caption="1fre" />
+
 
-
'''XNF7 BBOX, DEVELOPMENTAL PROTEIN, PH 7.5, 30 C, WITH ZINC, NMR, 1 STRUCTURE'''<br />
+
{{Structure
 +
|PDB= 1fre |SIZE=350|CAPTION= <scene name='initialview01'>1fre</scene>
 +
|SITE= <scene name='pdbsite=ZN1:Zn+Binding+Site+1'>ZN1</scene>
 +
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''XNF7 BBOX, DEVELOPMENTAL PROTEIN, PH 7.5, 30 C, WITH ZINC, NMR, 1 STRUCTURE'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
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 <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=ZN1:Zn+Binding+Site+1'>ZN1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FRE OCA].
+
1FRE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FRE OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8846787 8846787]
+
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:[http://www.ncbi.nlm.nih.gov/pubmed/8846787 8846787]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
Line 22: Line 31:
[[Category: zinc-binding protein]]
[[Category: zinc-binding protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:41:52 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:12:58 2008''

Revision as of 09:13, 20 March 2008


PDB ID 1fre

Drag the structure with the mouse to rotate
Sites:
Ligands:
Coordinates: save as pdb, mmCIF, xml



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. 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 Thu Mar 20 11:12:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools