6kyi | pdb_00006kyi

Rice Rubisco in complex with sulfate ions

spinqualitylabelsall models 6kyi, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6kyi is a 4 chain structure with sequence from Oryza sativa and Oryza sativa Japonica Group. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Ligands: GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RBL_ORYSA RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site (By similarity). Publication Abstract from PubMed Photosynthetic rate at the present atmospheric condition is limited by the CO2-fixing-enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) because of its extremely low catalytic rate (kcat) and poor affinity for CO2 (Kc) and specificity for CO2 (Sc/o). Rubisco in C4 plants generally shows higher kcat than that in C3 plants. Rubisco consists of eight large subunits and eight small subunits (RbcS). Previously, the chimeric incorporation of sorghum C4-type RbcS significantly increased the kcat of Rubisco in a C3 plant, rice. In this study, we knocked out rice RbcS multigene family by CRISPR/Cas9 and completely replaced the rice RbcS with sorghum RbcS in rice Rubisco. Obtained hybrid-Rubisco showed almost C4-plant-like catalytic properties, i.e., higher kcat, higher Kc and lower Sc/o. Transgenic lines expressing the hybrid-Rubisco accumulated reduced levels of Rubisco, whereas these showed slight but significantly higher photosynthetic capacity and similar biomass production under high CO2 condition compared to wild-type rice. High-resolution crystal structural analysis of the wild-type Rubisco and hybrid-Rubisco revealed the structural differences around the central pore of Rubisco and the betaC-betaD hairpin in RbcS. We speculate that such differences, particularly in the betaC-betaD hairpin, may impact the flexibility of Rubisco catalytic site and change the catalytic properties. Hybrid Rubisco with Complete Replacement of Rice Rubisco Small Subunits by Sorghum Counterparts Confers C4-Plant-like High Catalytic Activity.,Matsumura H, Shiomi K, Yamamoto A, Taketani Y, Kobayashi N, Yoshizawa T, Tanaka SI, Yoshikawa H, Endo M, Fukayama H Mol Plant. 2020 Aug 24. pii: S1674-2052(20)30268-9. doi:, 10.1016/j.molp.2020.08.012. PMID:32882392 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also RuBisCO 3D structures

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