1qbj
From Proteopedia
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|PDB= 1qbj |SIZE=350|CAPTION= <scene name='initialview01'>1qbj</scene>, resolution 2.1Å | |PDB= 1qbj |SIZE=350|CAPTION= <scene name='initialview01'>1qbj</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qbj OCA], [http://www.ebi.ac.uk/pdbsum/1qbj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qbj RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
The editing enzyme double-stranded RNA adenosine deaminase includes a DNA binding domain, Zalpha, which is specific for left-handed Z-DNA. The 2.1 angstrom crystal structure of Zalpha complexed to DNA reveals that the substrate is in the left-handed Z conformation. The contacts between Zalpha and Z-DNA are made primarily with the "zigzag" sugar-phosphate backbone, which provides a basis for the specificity for the Z conformation. A single base contact is observed to guanine in the syn conformation, characteristic of Z-DNA. Intriguingly, the helix-turn-helix motif, frequently used to recognize B-DNA, is used by Zalpha to contact Z-DNA. | The editing enzyme double-stranded RNA adenosine deaminase includes a DNA binding domain, Zalpha, which is specific for left-handed Z-DNA. The 2.1 angstrom crystal structure of Zalpha complexed to DNA reveals that the substrate is in the left-handed Z conformation. The contacts between Zalpha and Z-DNA are made primarily with the "zigzag" sugar-phosphate backbone, which provides a basis for the specificity for the Z conformation. A single base contact is observed to guanine in the syn conformation, characteristic of Z-DNA. Intriguingly, the helix-turn-helix motif, frequently used to recognize B-DNA, is used by Zalpha to contact Z-DNA. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Dyschromatosis symmetrica hereditaria OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601059 601059]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: protein/z-dna complex]] | [[Category: protein/z-dna complex]] | ||
| - | ''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 23:11:29 2008'' |
Revision as of 20:11, 30 March 2008
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| , resolution 2.1Å | |||||||
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| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE ZALPHA Z-DNA COMPLEX
Overview
The editing enzyme double-stranded RNA adenosine deaminase includes a DNA binding domain, Zalpha, which is specific for left-handed Z-DNA. The 2.1 angstrom crystal structure of Zalpha complexed to DNA reveals that the substrate is in the left-handed Z conformation. The contacts between Zalpha and Z-DNA are made primarily with the "zigzag" sugar-phosphate backbone, which provides a basis for the specificity for the Z conformation. A single base contact is observed to guanine in the syn conformation, characteristic of Z-DNA. Intriguingly, the helix-turn-helix motif, frequently used to recognize B-DNA, is used by Zalpha to contact Z-DNA.
About this Structure
1QBJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the Zalpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA., Schwartz T, Rould MA, Lowenhaupt K, Herbert A, Rich A, Science. 1999 Jun 11;284(5421):1841-5. PMID:10364558
Page seeded by OCA on Sun Mar 30 23:11:29 2008
