2KFP
Solution NMR structure of PSPTO_3016 from Pseudomonas syringae. Northeast Structural Genomics Consortium target PsR293.
Summary for 2KFP
| Entry DOI | 10.2210/pdb2kfp/pdb |
| NMR Information | BMRB: 16186 |
| Descriptor | PSPTO_3016 protein (1 entity in total) |
| Functional Keywords | alpha, beta, double-wing, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, nesg, unknown function |
| Biological source | Pseudomonas syringae |
| Total number of polymer chains | 1 |
| Total formula weight | 14829.89 |
| Authors | Feldmann, E.A.,Ramelot, T.A.,Zhao, L.,Hamilton, K.,Ciccosanti, C.,Xiao, R.,Nair, R.,Everett, J.K.,Swapna, G.,Acton, T.B.,Rost, B.,Montelione, G.T.,Kennedy, M.A.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2009-02-24, release date: 2009-03-24, Last modification date: 2024-05-08) |
| Primary citation | Feldmann, E.A.,Seetharaman, J.,Ramelot, T.A.,Lew, S.,Zhao, L.,Hamilton, K.,Ciccosanti, C.,Xiao, R.,Acton, T.B.,Everett, J.K.,Tong, L.,Montelione, G.T.,Kennedy, M.A. 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. J.Struct.Funct.Genom., 13:155-162, 2012 Cited by PubMed 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). PubMed: 22865330DOI: 10.1007/s10969-012-9140-8 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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