B3 domain

B3 domain

protein
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caption = B3 DNA binding domain of RAV1
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The B3 DNA binding domain (DBD) is a highly conserved domain exclusively found in transcription factors from higher plants (≥40 species) (Pfam|PF02362) combined with other domains (InterPro|IPR003340). It consists of 100-120 residues, includes seven beta strands and two alpha helices which form a DNA-binding pseudobarrel protein fold (SCOP|117343); interacts with the major groove of DNA.

B3 families

In "Arabidopsis thaliana" there are three main families of transcription factors which contain B3 domain:cite journal | author = Riechmann JL, Heard J, Martin G, Reuber L, Jiang C, Keddie J, Adam L, Pineda O, Ratcliffe OJ, Samaha RR, Creelman R, Pilgrim M, Broun P, Zhang JZ, Ghandehari D, Sherman BK, Yu G | title = Arabidopsis transcription factors: genome-wide comparative analysis among eukaryotes | journal = Science | volume = 290 | issue = 5499 | pages = 2105-10 | year = 2000 | pmid = 11118137 | doi = 10.1126/science.290.5499.2105 | issn = ]
* ARF (Auxin Respose Factors)
* ABI3 (ABscisic acid Insensitive3)
* RAV (Related to ABI3/VP1)

PDB|1WIDcite journal | author = Yamasaki K, Kigawa T, Inoue M, Tateno M, Yamasaki T, Yabuki T, Aoki M, Seki E, Matsuda T, Tomo Y, Hayami N, Terada T, Shirouzu M, Osanai T, Tanaka A, Seki M, Shinozaki K, Yokoyama S | title = Solution structure of the B3 DNA binding domain of the Arabidopsis cold-responsive transcription factor RAV1 | journal = Plant Cell | volume = 16 | issue = 12 | pages = 3448-59 | year = 2004 | pmid = 15548737 | doi = 10.1105/tpc.104.026112 | issn = ] and PDB|1YELcite journal | author = Waltner, J.K., Peterson, F.C., Lytle, B.L., Volkman, B.F. | title = Structure of the B3 domain from Arabidopsis thaliana protein At1g16640 | journal = Protein Sci | volume = 14 | issue = 9 | pages = 2478-83 | year = 2005 | pmid = 16081658 | doi = 10.1110/ps.051606305 ] are only known NMR solution phase structures of the B3 DNA Binding Domain.

Related proteins

The N-terminal domain of restriction endonuclease EcoRII; the C-terminal domain of restriction endonuclease BfiI possess a similar DNA-binding pseudobarrel protein fold.cite journal | author = Zhou XE, Wang Y, Reuter M, Mücke M, Krüger DH, Meehan EJ, Chen L | title = Crystal structure of type IIE restriction endonuclease EcoRII reveals an autoinhibition mechanism by a novel effector-binding fold | journal = J. Mol. Biol. | volume = 335 | issue = 1 | pages = 307-19 | year = 2004 | pmid = 14659759 | doi = 10.1016/j.jmb.2003.10.030 | issn = ] cite journal | author = Grazulis S, Manakova E, Roessle M, Bochtler M, Tamulaitiene G, Huber R, Siksnys V | title = Structure of the metal-independent restriction enzyme BfiI reveals fusion of a specific DNA-binding domain with a nonspecific nuclease | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 102 | issue = 44 | pages = 15797-802 | year = 2005 | pmid = 16247004 | doi = 10.1073/pnas.0507949102 | issn = ]

See also

*Restriction endonuclease EcoRII
*Auxin
*Abscisic acid

References

External links

* [http://transcriptionfactor.org/ DBD database of predicted transcription factors] cite journal | author = Kummerfeld SK, Teichmann SA. | title = DBD: a transcription factor prediction database | journal = Nucleic Acids Res. | volume = 34 | issue = Database issue | pages = D74-81 | year = 2006 | pmid = 16381825 | doi = 10.1093/nar/gkj131 ] Uses a curated set of DNA-binding domains to predict transcription factors in all completely sequenced genomes
*Classification in the "Transcription factors" table according to the [http://www.gene-regulation.com/pub/databases/transfac/cl.html Transfac] database.
* [http://attfdb.cbi.pku.edu.cn/browsefamily.php?familyname=B3 Database of Arabidopsis Transcription Factors]


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