Catalytic roles of flexible regions at the active site of ribulose-bisphosphate carboxylase/oxygenase (Rubisco)

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Chemical and mutagenesis studies of Rubisco have identified Lys329 and Glu48 as active-site residues that are located in distinct, interacting domains from adjacent subunits. Crystallographic analyses have shown that Lys329 is the apical residue in a 12-residue flexible loop (loop 6) of the {Beta},{alpha}-barrel domain of the active site and that Glu48 resides at the end of helix B of the N-terminal domain of the active site. When phosphorylated ligands are bound by the enzyme, loop 6 adopts a closed conformation and, in concert with repositioning of helix B, thereby occludes the active site from the external environment. In this ... continued below

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6 p.

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Hartman, F.C.; Harpel, M.R.; Chen, Yuh-Ru; Larson, E.M. & Larimer, F.W. December 31, 1995.

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Chemical and mutagenesis studies of Rubisco have identified Lys329 and Glu48 as active-site residues that are located in distinct, interacting domains from adjacent subunits. Crystallographic analyses have shown that Lys329 is the apical residue in a 12-residue flexible loop (loop 6) of the {Beta},{alpha}-barrel domain of the active site and that Glu48 resides at the end of helix B of the N-terminal domain of the active site. When phosphorylated ligands are bound by the enzyme, loop 6 adopts a closed conformation and, in concert with repositioning of helix B, thereby occludes the active site from the external environment. In this closed conformation, the {gamma}-carboxylate of Glu48 and the {epsilon}-amino group of Lys329 engage in intersubunit electrostatic interaction. By use of appropriate site-directed mutants of Rhodospirillum rubrum Rubisco, we are addressing several issues: the catalytic roles of Lys329 and Glu48, the functional significance of the intersubunit salt bridge comprised of these two residues, and the roles of loop 6 and helix B in stabilizing labile reaction intermediates. Characterization of novel products derived from misprocessing of D-ribulose-1,5-bisphosphate (RuBP) by the mutant proteins have illuminated the structure of the key intermediate in the normal oxygenase pathway.

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6 p.

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OSTI as DE96004399

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  • 10. international photosynthesis congress, Montpellier (France), 20-25 Aug 1995

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  • Other: DE96004399
  • Report No.: CONF-9508202--1
  • Grant Number: AC05-84OR21400
  • Office of Scientific & Technical Information Report Number: 205848
  • Archival Resource Key: ark:/67531/metadc664942

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  • December 31, 1995

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  • June 29, 2015, 9:42 p.m.

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  • Jan. 25, 2016, 12:10 p.m.

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Hartman, F.C.; Harpel, M.R.; Chen, Yuh-Ru; Larson, E.M. & Larimer, F.W. Catalytic roles of flexible regions at the active site of ribulose-bisphosphate carboxylase/oxygenase (Rubisco), article, December 31, 1995; Tennessee. (digital.library.unt.edu/ark:/67531/metadc664942/: accessed August 17, 2017), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.