5olk

Crystal structure of the ATP-cone-containing NrdB from Leeuwenhoekiella blandensis

spinqualitylabelsall models 5olk, resolution 2.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5olk is a 4 chain structure with sequence from Leeuwenhoekiella blandensis MED217. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.45Å Ligands: DTP, MG, MN, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A3XHF9_LEEBM Publication Abstract from PubMed Ribonucleotide reductases (RNRs) are key enzymes in DNA metabolism, with allosteric mechanisms controlling substrate specificity and overall activity. In RNRs, the activity master-switch, the ATP-cone, has been found exclusively in the catalytic subunit. In two class I RNR subclasses whose catalytic subunit lacks the ATP-cone, we discovered ATP-cones in the radical-generating subunit. The ATP-cone in the Leeuwenhoekiella blandensis radical-generating subunit regulates activity via quaternary structure induced by binding of nucleotides. ATP induces enzymatically competent dimers, whereas dATP induces non-productive tetramers, resulting in different holoenzymes. The tetramer forms by interactions between ATP-cones, shown by a 2.45 A crystal structure. We also present evidence for an Mn(III)Mn(IV) metal center. In summary, lack of an ATP-cone domain in the catalytic subunit was compensated by transfer of the domain to the radical-generating subunit. To our knowledge, this represents the first observation of transfer of an allosteric domain between components of the same enzyme complex. Novel ATP-cone-driven allosteric regulation of ribonucleotide reductase via the radical-generating subunit.,Rozman Grinberg I, Lundin D, Hasan M, Crona M, Jonna VR, Loderer C, Sahlin M, Markova N, Borovok I, Berggren G, Hofer A, Logan DT, Sjoberg BM Elife. 2018 Feb 1;7. pii: 31529. doi: 10.7554/eLife.31529. PMID:29388911 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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