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2adr
From Proteopedia
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|PDB= 2adr |SIZE=350|CAPTION= <scene name='initialview01'>2adr</scene> | |PDB= 2adr |SIZE=350|CAPTION= <scene name='initialview01'>2adr</scene> | ||
|SITE= <scene name='pdbsite=ZNC:Zn+Finger+2'>ZNC</scene> | |SITE= <scene name='pdbsite=ZNC:Zn+Finger+2'>ZNC</scene> | ||
| - | |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=2adr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2adr OCA], [http://www.ebi.ac.uk/pdbsum/2adr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2adr RCSB]</span> | ||
}} | }} | ||
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[[Category: Bowers, P M.]] | [[Category: Bowers, P M.]] | ||
[[Category: Kleivt, R E.]] | [[Category: Kleivt, R E.]] | ||
| - | [[Category: ZN]] | ||
[[Category: adr1]] | [[Category: adr1]] | ||
[[Category: nmr]] | [[Category: nmr]] | ||
| Line 30: | Line 32: | ||
[[Category: zinc finger]] | [[Category: zinc finger]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:51:17 2008'' |
Revision as of 22:51, 30 March 2008
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ADR1 DNA-BINDING DOMAIN FROM SACCHAROMYCES CEREVISIAE, NMR, 25 STRUCTURES
Overview
The region responsible for sequence-specific DNA binding by the transcription factor ADR1 contains two Cys2-His2 zinc fingers and an additional N-terminal proximal accessory region (PAR). The N-terminal (non-finger) PAR is unstructured in the absence of DNA and undergoes a folding transition on binding the DNA transcription target site. We have used a set of HN-HN NOEs derived from a perdeuterated protein-DNA complex to describe the fold of ADR1 bound to the UAS1 binding site. The PAR forms a compact domain consisting of three antiparallel strands that contact A-T base pairs in the major groove. The three-strand domain is a novel fold among all known DNA-binding proteins. The PAR shares sequence homology with the N-terminal regions of other zinc finger proteins, suggesting that it represents a new DNA-binding module that extends the binding repertoire of zinc finger proteins.
About this Structure
2ADR is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
A folding transition and novel zinc finger accessory domain in the transcription factor ADR1., Bowers PM, Schaufler LE, Klevit RE, Nat Struct Biol. 1999 May;6(5):478-85. PMID:10331877
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