Structure of the B3 domain from Arabidopsis thaliana protein At1g16640.

ABSTRACT: A novel DNA binding motif, the B3 domain, has been identified in a number of transcription factors specific to higher plant species, and was recently found to define a new protein fold. Here we report the second structure of a B3 domain, that of the Arabidopsis thaliana protein, At1g16640. As part of an effort to 'rescue' structural genomics targets deemed unsuitable for structure determination as full-length proteins, we applied a combined bioinformatic and experimental strategy to identify an optimal construct containing a predicted conserved domain. By screening a series of N- and C-terminally truncated At1g16640 fragments, we isolated a stable folded domain that met our criteria for structural analysis by NMR spectroscopy. The structure of the B3 domain of At1g16640 consists of a seven

SUBMITTER: Waltner JK 

PROVIDER: S-EPMC2253459 | biostudies-literature | 2005 Sep

REPOSITORIES: biostudies-literature