3o5t | pdb_00003o5t

Structure of DraG-GlnZ complex with ADP

spinqualitylabelsall models 3o5t, resolution 2.09Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3o5t is a 2 chain structure with sequence from Azospirillum brasilense. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, MG Gene: draG (Azospirillum brasilense), glnZ (Azospirillum brasilense) Activity: [dinitrogen_reductase_hydrolase ADP-ribosyl-[dinitrogen reductase] hydrolase], with EC number 3.2.2.24 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Nitrogen metabolism in bacteria and archaea is regulated by a ubiquitous class of proteins belonging to the P(II)family. P(II) proteins act as sensors of cellular nitrogen, carbon, and energy levels, and they control the activities of a wide range of target proteins by protein-protein interaction. The sensing mechanism relies on conformational changes induced by the binding of small molecules to P(II) and also by P(II) posttranslational modifications. In the diazotrophic bacterium Azospirillum brasilense, high levels of extracellular ammonium inactivate the nitrogenase regulatory enzyme DraG by relocalizing it from the cytoplasm to the cell membrane. Membrane localization of DraG occurs through the formation of a ternary complex in which the P(II) protein GlnZ interacts simultaneously with DraG and the ammonia channel AmtB. Here we describe the crystal structure of the GlnZ-DraG complex at 2.1 A resolution, and confirm the physiological relevance of the structural data by site-directed mutagenesis. In contrast to other known P(II) complexes, the majority of contacts with the target protein do not involve the T-loop region of P(II). Hence this structure identifies a different mode of P(II) interaction with a target protein and demonstrates the potential for P(II) proteins to interact simultaneously with two different targets. A structural model of the AmtB-GlnZ-DraG ternary complex is presented. The results explain how the intracellular levels of ATP, ADP, and 2-oxoglutarate regulate the interaction between these three proteins and how DraG discriminates GlnZ from its close paralogue GlnB. Crystal structure of the GlnZ-DraG complex reveals a different form of PII-target interaction.,Rajendran C, Gerhardt EC, Bjelic S, Gasperina A, Scarduelli M, Pedrosa FO, Chubatsu LS, Merrick M, Souza EM, Winkler FK, Huergo LF, Li XD Proc Natl Acad Sci U S A. 2011 Nov 22;108(47):18972-6. Epub 2011 Nov 9. PMID:22074780 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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