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Title: Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis

Authors:
; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ;  [1];  [2];  [2] more »;  [2];  [2];  [2] « less
  1. Columbia
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
National Institutes of Health (NIH)
OSTI Identifier:
1234760
Resource Type:
Journal Article
Resource Relation:
Journal Name: Nature Communications; Journal Volume: 7; Journal Issue: 01, 2016
Country of Publication:
United States
Language:
ENGLISH

Citation Formats

Ardiccioni, Chiara, Clarke, Oliver B., Tomasek, David, Issa, Habon A., von Alpen, Desiree C., Pond, Heather L., Banerjee, Surajit, Rajashankar, Kanagalaghatta R., Liu, Qun, Guan, Ziqiang, Li, Chijun, Kloss, Brian, Bruni, Renato, Kloppmann, Edda, Rost, Burkhard, Manzini, M. Chiara, Shapiro, Lawrence, Mancia, Filippo, BNL), GWU), Cornell), Duke-MED), and NYSBC). Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis. United States: N. p., 2016. Web. doi:10.1038/ncomms10175.
Ardiccioni, Chiara, Clarke, Oliver B., Tomasek, David, Issa, Habon A., von Alpen, Desiree C., Pond, Heather L., Banerjee, Surajit, Rajashankar, Kanagalaghatta R., Liu, Qun, Guan, Ziqiang, Li, Chijun, Kloss, Brian, Bruni, Renato, Kloppmann, Edda, Rost, Burkhard, Manzini, M. Chiara, Shapiro, Lawrence, Mancia, Filippo, BNL), GWU), Cornell), Duke-MED), & NYSBC). Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis. United States. doi:10.1038/ncomms10175.
Ardiccioni, Chiara, Clarke, Oliver B., Tomasek, David, Issa, Habon A., von Alpen, Desiree C., Pond, Heather L., Banerjee, Surajit, Rajashankar, Kanagalaghatta R., Liu, Qun, Guan, Ziqiang, Li, Chijun, Kloss, Brian, Bruni, Renato, Kloppmann, Edda, Rost, Burkhard, Manzini, M. Chiara, Shapiro, Lawrence, Mancia, Filippo, BNL), GWU), Cornell), Duke-MED), and NYSBC). 2016. "Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis". United States. doi:10.1038/ncomms10175.
@article{osti_1234760,
title = {Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis},
author = {Ardiccioni, Chiara and Clarke, Oliver B. and Tomasek, David and Issa, Habon A. and von Alpen, Desiree C. and Pond, Heather L. and Banerjee, Surajit and Rajashankar, Kanagalaghatta R. and Liu, Qun and Guan, Ziqiang and Li, Chijun and Kloss, Brian and Bruni, Renato and Kloppmann, Edda and Rost, Burkhard and Manzini, M. Chiara and Shapiro, Lawrence and Mancia, Filippo and BNL) and GWU) and Cornell) and Duke-MED) and NYSBC)},
abstractNote = {},
doi = {10.1038/ncomms10175},
journal = {Nature Communications},
number = 01, 2016,
volume = 7,
place = {United States},
year = 2016,
month = 6
}
  • No abstract prepared.
  • Phosphoenolpyruvate carboxykinase catalyzes the reversible decarboxylation of oxaloacetic acid with the concomitant transfer of the {gamma}-phosphate of GTP to form PEP and GDP as the first committed step of gluconeogenesis and glyceroneogenesis. The three structures of the mitochondrial isoform of PEPCK reported are complexed with Mn{sup 2+}, Mn{sup 2+}-PEP, or Mn{sup 2+}-malonate-Mn{sup 2+}GDP and provide the first observations of the structure of the mitochondrial isoform and insight into the mechanism of catalysis mediated by this enzyme. The structures show the involvement of the hyper-reactive cysteine (C307) in the coordination of the active site Mn{sup 2+}. Upon formation of the PEPCK-Mn{supmore » 2+}-PEP or PEPCK-Mn{sup 2+}-malonate-Mn{sup 2+}GDP complexes, C307 coordination is lost as the P-loop in which it resides adopts a different conformation. The structures suggest that stabilization of the cysteine-coordinated metal geometry holds the enzyme as a catalytically incompetent metal complex and may represent a previously unappreciated mechanism of regulation. A third conformation of the mobile P-loop in the PEPCK-Mn{sup 2+}-malonate-Mn{sup 2+}GDP complex demonstrates the participation of a previously unrecognized, conserved serine residue (S305) in mediating phosphoryl transfer. The ordering of the mobile active site lid in the PEPCK-Mn{sup 2+}-malonate-Mn{sup 2+}GDP complex yields the first observation of this structural feature and provides additional insight into the mechanism of phosphoryl transfer.« less
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