caa a22 4500 397520484 CHVBK 20180308164631.0 cr unu---uuuuu 161202e199509 xx s 000 0 eng 10.1093/jxb/46.special_issue.1261 doi (NATIONALLICENCE)oxford-10.1093/jxb/46.special_issue.1261 The crystal structures of Rubisco and opportunities for manipulating photosynthesis [Elektronische Daten] [Steven Gutteridge, Janet Newman, Chuck Herrmann, Dan Rhoades] The crystal structures of four species of Rubisco in a number of complexes have been solved to high resolution. The data have been used with some success to rationalize mutagenesis strategies, identify residues involved in the reaction cycle and, of particular concern, understand the basis for the ability of these enzymes to discriminate differentially between CO2 and O2. However, a detailed comparison of these structures indicates that there are significant differences in the positions of critical regions of the protein that may influence the outcome of catalysis and have certainly influenced the conclusions of investigators. For example, the C-terminus of the L-subunit of the inactive dimeric enzyme from Rhodospirillum rubrum has a quite distinct motif compared to the same segment of the activated hexadecameric Rubisco from cyanobacteria or plants. It is plausible that this is yet one more region of the protein that adopts different conformations depending on whether the active site is vacant or occupied by co-factors, bisphosphate substrate or analogues. © 1995 Oxford University Press Photosynthetic Carbon Reduction nationallicence Rubisco nationallicence active site nationallicence protein conformation nationallicence Gutteridge Steven Central Research and Development Department, Experimental Station DuPont Company, Wilmington, DE 19880, USA aut Newman Janet Department of Molecular Biophysics, Columbia Medical School New York, NY, USA aut Herrmann Chuck Central Research and Development Department, Experimental Station DuPont Company, Wilmington, DE 19880, USA aut Rhoades Dan Central Research and Development Department, Experimental Station DuPont Company, Wilmington, DE 19880, USA aut Journal of Experimental Botany Oxford University Press 46/special_issue(1995-09), 1261-1267 0022-0957 46:special_issue<1261 1995 46 exbotj https://doi.org/10.1093/jxb/46.special_issue.1261 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/jxb/46.special_issue.1261 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Gutteridge Steven Central Research and Development Department, Experimental Station DuPont Company, Wilmington, DE 19880, USA aut NATIONALLICENCE 700 1- Newman Janet Department of Molecular Biophysics, Columbia Medical School New York, NY, USA aut NATIONALLICENCE 700 1- Herrmann Chuck Central Research and Development Department, Experimental Station DuPont Company, Wilmington, DE 19880, USA aut NATIONALLICENCE 700 1- Rhoades Dan Central Research and Development Department, Experimental Station DuPont Company, Wilmington, DE 19880, USA aut NATIONALLICENCE 773 0- Journal of Experimental Botany Oxford University Press 46/special_issue(1995-09), 1261-1267 0022-0957 46:special_issue<1261 1995 46 exbotj Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford