3NEK
Crystal structure of a nitrogen repressor-like protein MJ0159 from Methanococcus jannaschii
Replaces: 2QYXSummary for 3NEK
| Entry DOI | 10.2210/pdb3nek/pdb |
| Descriptor | nitrogen repressor-like protein MJ0159, GLYCEROL (3 entities in total) |
| Functional Keywords | structural genomics, unknown function, psi-2, protein structure initiative, new york sgx research center for structural genomics, nysgxrc |
| Biological source | Methanocaldococcus jannaschii (Methanococcus jannaschii) |
| Total number of polymer chains | 2 |
| Total formula weight | 54689.71 |
| Authors | Bonanno, J.B.,Patskovsky, Y.,Malashkevich, V.,Ozyurt, S.,Dickey, M.,Wu, B.,Maletic, M.,Rodgers, L.,Koss, J.,Sauder, J.M.,Burley, S.K.,Almo, S.C.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2010-06-09, release date: 2010-06-23, Last modification date: 2024-11-06) |
| Primary citation | Wisedchaisri, G.,Dranow, D.M.,Lie, T.J.,Bonanno, J.B.,Patskovsky, Y.,Ozyurt, S.A.,Sauder, J.M.,Almo, S.C.,Wasserman, S.R.,Burley, S.K.,Leigh, J.A.,Gonen, T. Structural underpinnings of nitrogen regulation by the prototypical nitrogen-responsive transcriptional factor NrpR. Structure, 18:1512-1521, 2010 Cited by PubMed Abstract: Plants and microorganisms reduce environmental inorganic nitrogen to ammonium, which then enters various metabolic pathways solely via conversion of 2-oxoglutarate (2OG) to glutamate and glutamine. Cellular 2OG concentrations increase during nitrogen starvation. We recently identified a family of 2OG-sensing proteins--the nitrogen regulatory protein NrpR--that bind DNA and repress transcription of nitrogen assimilation genes. We used X-ray crystallography to determine the structure of NrpR regulatory domain. We identified the NrpR 2OG-binding cleft and show that residues predicted to interact directly with 2OG are conserved among diverse classes of 2OG-binding proteins. We show that high levels of 2OG inhibit NrpRs ability to bind DNA. Electron microscopy analyses document that NrpR adopts different quaternary structures in its inhibited 2OG-bound state compared with its active apo state. Our results indicate that upon 2OG release, NrpR repositions its DNA-binding domains correctly for optimal interaction with DNA thereby enabling gene repression. PubMed: 21070950DOI: 10.1016/j.str.2010.08.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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