1co4
From Proteopedia
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|PDB= 1co4 |SIZE=350|CAPTION= <scene name='initialview01'>1co4</scene> | |PDB= 1co4 |SIZE=350|CAPTION= <scene name='initialview01'>1co4</scene> | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1co4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1co4 OCA], [http://www.ebi.ac.uk/pdbsum/1co4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1co4 RCSB]</span> | ||
}} | }} | ||
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[[Category: Winge, D R.]] | [[Category: Winge, D R.]] | ||
[[Category: Zawrotny, M E.]] | [[Category: Zawrotny, M E.]] | ||
- | [[Category: ZN]] | ||
[[Category: amt]] | [[Category: amt]] | ||
[[Category: metal regulation]] | [[Category: metal regulation]] | ||
[[Category: metallothionein]] | [[Category: metallothionein]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:25:16 2008'' |
Revision as of 16:25, 30 March 2008
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Ligands: | |||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
SOLUTION STRUCTURE OF A ZINC DOMAIN CONSERVED IN YEAST COPPER-REGULATED TRANSCRIPTION FACTORS
Overview
The three dimensional structure of the N-terminal domain (residues 1-42) of the copper-responsive transcription factor Amtl from Candida glabrata has been determined by two-dimensional 1H-correlated nuclear magnetic resonance (NMR) methods. The domain contains an array of zinc-binding residues (Cys-X2-Cys-X8-Cys-X-His) that is conserved among a family of Cu-responsive transcription factors. The structure is unlike those of previously characterized zinc finger motifs, and consists of a three-stranded antiparallel beta-sheet with two short helical segments that project from one end of the beta-sheet. Conserved residues at positions 16, 18 and 19 form a basic patch that may be important for DNA binding.
About this Structure
1CO4 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Solution structure of a zinc domain conserved in yeast copper-regulated transcription factors., Turner RB, Smith DL, Zawrotny ME, Summers MF, Posewitz MC, Winge DR, Nat Struct Biol. 1998 Jul;5(7):551-5. PMID:9665167
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