Catalytic Core of a Membrane-Associated Eukaryotic Polyphosphate Polymerase Export

@article{citeulike:4395117, abstract = {Polyphosphate (polyP) occurs ubiquitously in cells, but its functions are poorly understood and its synthesis has only been characterized in bacteria. Using x-ray crystallography, we identified a eukaryotic polyphosphate polymerase within the membrane-integral vacuolar transporter chaperone (VTC) complex. A 2.6 angstrom crystal structure of the catalytic domain grown in the presence of adenosine triphosphate (ATP) reveals polyP winding through a tunnel-shaped pocket. Nucleotide- and phosphate-bound structures suggest that the enzyme functions by metal-assisted cleavage of the ATP {gamma}-phosphate, which is then in-line transferred to an acceptor phosphate to form polyP chains. Mutational analysis of the transmembrane domain indicates that VTC may integrate cytoplasmic polymer synthesis with polyP membrane translocation. Identification of the polyP-synthesizing enzyme opens the way to determine the functions of polyP in lower eukaryotes. 10.1126/science.1168120}, author = {Hothorn, Michael and Neumann, Heinz and Lenherr, Esther D. and Wehner, Mark and Rybin, Vladimir and Hassa, Paul O. and Uttenweiler, Andreas and Reinhardt, Monique and Schmidt, Andrea and Seiler, Jeanette and Ladurner, Andreas G. and Herrmann, Christian and Scheffzek, Klaus and Mayer, Andreas}, citeulike-article-id = {4395117}, citeulike-linkout-0 = {http://dx.doi.org/10.1126/science.1168120}, citeulike-linkout-1 = {http://www.sciencemag.org/cgi/content/abstract/324/5926/513}, day = {24}, doi = {10.1126/science.1168120}, journal = {Science}, keywords = {cesa}, month = {April}, number = {5926}, pages = {513--516}, posted-at = {2009-04-24 12:56:40}, priority = {2}, title = {Catalytic Core of a Membrane-Associated Eukaryotic Polyphosphate Polymerase}, url = {http://dx.doi.org/10.1126/science.1168120}, volume = {324}, year = {2009} }

TY - JOUR ID - citeulike:4395117 L3 - citeulike-article-id:4395117 N2 - Polyphosphate (polyP) occurs ubiquitously in cells, but its functions are poorly understood and its synthesis has only been characterized in bacteria. Using x-ray crystallography, we identified a eukaryotic polyphosphate polymerase within the membrane-integral vacuolar transporter chaperone (VTC) complex. A 2.6 angstrom crystal structure of the catalytic domain grown in the presence of adenosine triphosphate (ATP) reveals polyP winding through a tunnel-shaped pocket. Nucleotide- and phosphate-bound structures suggest that the enzyme functions by metal-assisted cleavage of the ATP {gamma}-phosphate, which is then in-line transferred to an acceptor phosphate to form polyP chains. Mutational analysis of the transmembrane domain indicates that VTC may integrate cytoplasmic polymer synthesis with polyP membrane translocation. Identification of the polyP-synthesizing enzyme opens the way to determine the functions of polyP in lower eukaryotes. 10.1126/science.1168120 IS - 5926 JF - Science EP - 516 TI - Catalytic Core of a Membrane-Associated Eukaryotic Polyphosphate Polymerase VL - 324 SP - 513 KW - cesa AU - Hothorn, Michael AU - Neumann, Heinz AU - Lenherr, Esther AU - Wehner, Mark AU - Rybin, Vladimir AU - Hassa, Paul AU - Uttenweiler, Andreas AU - Reinhardt, Monique AU - Schmidt, Andrea AU - Seiler, Jeanette AU - Ladurner, Andreas AU - Herrmann, Christian AU - Scheffzek, Klaus AU - Mayer, Andreas PY - 2009/04/24/ UR - http://dx.doi.org/10.1126/science.1168120 ER -