4rf9 | pdb_00004rf9

Crystal structure of double-domain arginine kinase from Anthopleura japonicas in complex with L-arginine and ATPgS

spinqualitylabelsall models 4rf9, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4rf9 is a 2 chain structure with sequence from Anthopleura japonica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.35Å Ligands: ACT, AGS, ARG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function KARG_ANTJA Publication Abstract from PubMed Tandem duplications and fusions of single genes have led to magnificent expansions in the divergence of protein structures and functions over evolutionary timescales. One of the possible results is polydomain enzymes with interdomain cooperativities, few examples of which have been structurally characterized at the full-length level to explore their innate synergistic mechanisms. This work reports the crystal structures of a double-domain phosphagen kinase in both apo and ligand-bound states, revealing a novel asymmetric L-shaped arrangement of the two domains. Unexpectedly, the interdomain connections are not based on a flexible hinge linker but on a rigid secondary-structure element: a long alpha-helix that tethers the tandem domains in relatively fixed positions. Besides the connective helix, the two domains also contact each other directly and form an interdomain interface in which hydrogen bonds and hydrophobic interactions further stabilize the L-shaped domain arrangement. Molecular-dynamics simulations show that the interface is generally stable, suggesting that the asymmetric domain arrangement crystallographically observed in the present study is not a conformational state simply restrained by crystal-packing forces. It is possible that the asymmetrically arranged tandem domains could provide a structural basis for further studies of the interdomain synergy. Structure of a double-domain phosphagen kinase reveals an asymmetric arrangement of the tandem domains.,Wang Z, Qiao Z, Ye S, Zhang R Acta Crystallogr D Biol Crystallogr. 2015 Apr;71(Pt 4):779-89. doi:, 10.1107/S1399004715001169. Epub 2015 Mar 26. PMID:25849389 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Arginine kinase 3D structures

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