This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The DJ-1 superfamily is a large and diverse set of proteins that has representatives in most kingdoms of life. Human DJ-1 is protein that protects cells against oxidative stress, and in implicated in both Parkinson?s disease and certain types of cancer. Many other members of the DJ-1 superfamily have been partially characterized and play important roles in the response of various organisms to environmental stress. We are interested in determining 1) how related but functionally distinct proteins in the DJ-1 superfamily use the similar structural features to fulfill different biological roles and 2) how posttranslational modifications regulate the functions of these proteins. We are studying DJ-1 from several species (Human, Drosophila melanogaster, Escherichia coli), a related protein from Pseudomomas fluorescens that functions as an isonitrile hydratase, and several general stress response proteins in the DJ-1 superfamily. We and our collaborators have shown that the Drosophila melanogaster and E. coli DJ-1 homologues are functionally interchangeable with the human protein, and will use structural information to determine how these disease-related proteins are regulated. In a related project, we have shown that isonitrile hydratase catalyzes the conversion of various isonitriles to amides and employs amino acids that are well-conserved in the DJ-1 superfamily to accomplish this unique chemistry. We are also investigating the structures of an unusual clade of plant-specific DJ-1 proteins that are composed of two fused DJ-1-like domains. We have collected datasets on crystals of each of these proteins using the rotating anode source at UNL. Each of these structures has been successfully solved by molecular replacement and the improved data that we will collect at the APS will aid in model refinement, analysis, and publication.
| Weingarten, Adam S; Dannenhoffer, Adam J; Kazantsev, Roman V et al. (2018) Chromophore Dipole Directs Morphology and Photocatalytic Hydrogen Generation. J Am Chem Soc 140:4965-4968 |
| Yang, Cheolhee; Choi, Minseo; Kim, Jong Goo et al. (2018) Protein Structural Dynamics of Wild-Type and Mutant Homodimeric Hemoglobin Studied by Time-Resolved X-Ray Solution Scattering. Int J Mol Sci 19: |
| Kazantsev, Roman V; Dannenhoffer, Adam J; Weingarten, Adam S et al. (2017) Crystal-Phase Transitions and Photocatalysis in Supramolecular Scaffolds. J Am Chem Soc 139:6120-6127 |
| Fournier, Bertrand; Sokolow, Jesse; Coppens, Philip (2016) Analysis of multicrystal pump-probe data sets. II. Scaling of ratio data sets. Acta Crystallogr A Found Adv 72:250-60 |
| Cho, Hyun Sun; Schotte, Friedrich; Dashdorj, Naranbaatar et al. (2016) Picosecond Photobiology: Watching a Signaling Protein Function in Real Time via Time-Resolved Small- and Wide-Angle X-ray Scattering. J Am Chem Soc 138:8815-23 |
| Pande, Kanupriya; Hutchison, Christopher D M; Groenhof, Gerrit et al. (2016) Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein. Science 352:725-9 |
| Weingarten, Adam S; Kazantsev, Roman V; Palmer, Liam C et al. (2015) Supramolecular Packing Controls H? Photocatalysis in Chromophore Amphiphile Hydrogels. J Am Chem Soc 137:15241-6 |
| Pfoh, Roland; Pai, Emil F; Saridakis, Vivian (2015) Nicotinamide mononucleotide adenylyltransferase displays alternate binding modes for nicotinamide nucleotides. Acta Crystallogr D Biol Crystallogr 71:2032-9 |
| Mariette, Céline; Guérin, Laurent; Rabiller, Philippe et al. (2015) The creation of modulated monoclinic aperiodic composites in n-alkane/urea compounds. Z Kristallogr Cryst Mater 230:5-11 |
| Yang, Xiaojing; Stojkovi?, Emina A; Ozarowski, Wesley B et al. (2015) Light Signaling Mechanism of Two Tandem Bacteriophytochromes. Structure 23:1179-89 |
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