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J Struct Funct Genomics. 2012 Sep;13(3):155-62. doi: 10.1007/s10969-012-9140-8. Epub 2012 Aug 3.

Solution NMR and X-ray crystal structures of Pseudomonas syringae Pspto_3016 from protein domain family PF04237 (DUF419) adopt a "double wing" DNA binding motif.

Author information

1
Department of Chemistry and Biochemistry, Miami University, Oxford, OH 45056, USA.

Abstract

The protein Pspto_3016 is a 117-residue member of the protein domain family PF04237 (DUF419), which is to date a functionally uncharacterized family of proteins. In this report, we describe the structure of Pspto_3016 from Pseudomonas syringae solved by both solution NMR and X-ray crystallography at 2.5 Å resolution. In both cases, the structure of Pspto_3016 adopts a "double wing" α/β sandwich fold similar to that of protein YjbR from Escherichia coli and to the C-terminal DNA binding domain of the MotA transcription factor (MotCF) from T4 bacteriophage, along with other uncharacterized proteins. Pspto_3016 was selected by the Protein Structure Initiative of the National Institutes of Health and the Northeast Structural Genomics Consortium (NESG ID PsR293).

PMID:
22865330
PMCID:
PMC3697073
DOI:
10.1007/s10969-012-9140-8
[Indexed for MEDLINE]
Free PMC Article

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