2ITM
Crystal structure of the E. coli xylulose kinase complexed with xylulose
Summary for 2ITM
| Entry DOI | 10.2210/pdb2itm/pdb |
| Descriptor | Xylulose kinase, D-XYLULOSE, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | xylulokinase, xylulose, kinase, atpase, fggy kinase, transferase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 106046.88 |
| Authors | di Luccio, E.,Voegtli, J.,Wilson, D.K. (deposition date: 2006-10-19, release date: 2006-11-14, Last modification date: 2024-02-21) |
| Primary citation | Di Luccio, E.,Petschacher, B.,Voegtli, J.,Chou, H.T.,Stahlberg, H.,Nidetzky, B.,Wilson, D.K. Structural and kinetic studies of induced fit in xylulose kinase from Escherichia coli. J.Mol.Biol., 365:783-798, 2007 Cited by PubMed Abstract: The primary metabolic route for D-xylose, the second most abundant sugar in nature, is via the pentose phosphate pathway after a two-step or three-step conversion to xylulose-5-phosphate. Xylulose kinase (XK; EC 2.7.1.17) phosphorylates D-xylulose, the last step in this conversion. The apo and D-xylulose-bound crystal structures of Escherichia coli XK have been determined and show a dimer composed of two domains separated by an open cleft. XK dimerization was observed directly by a cryo-EM reconstruction at 36 A resolution. Kinetic studies reveal that XK has a weak substrate-independent MgATP-hydrolyzing activity, and phosphorylates several sugars and polyols with low catalytic efficiency. Binding of pentulose and MgATP to form the reactive ternary complex is strongly synergistic. Although the steady-state kinetic mechanism of XK is formally random, a path is preferred in which D-xylulose binds before MgATP. Modelling of MgATP binding to XK and the accompanying conformational change suggests that sugar binding is accompanied by a dramatic hinge-bending movement that enhances interactions with MgATP, explaining the observed synergism. A catalytic mechanism is proposed and supported by relevant site-directed mutants. PubMed: 17123542DOI: 10.1016/j.jmb.2006.10.068 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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