RuBisCO: Difference between revisions
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{{STRUCTURE_1rcx| PDB=1rcx | SIZE=400| SCENE= |right|CAPTION=Spinach RuBisCO 8 large and 8 small chains complex with substrate ribulose-1,5- bisphosphate, [[1rcx]] }} | {{STRUCTURE_1rcx| PDB=1rcx | SIZE=400| SCENE= |right|CAPTION=Spinach RuBisCO 8 large and 8 small chains complex with substrate ribulose-1,5- bisphosphate, [[1rcx]] }} | ||
'''Ribulose-1,5-bisphosphate carboxylase oxygenase – RuBisCO''' (RBCO) catalyzes the first step in carbon fixation, and it is the most abundant protein on earth. RBCO can either carboxylate or oxygenate ribulose-1,5-bisphosphate (RUBP) with CO<sub>2</sub> or O<sub>2</sub>, respectively. RBCO from flowering plants | '''Ribulose-1,5-bisphosphate carboxylase oxygenase – RuBisCO''' (RBCO) catalyzes the first step in photosynthetic carbon fixation, and it is the most abundant protein on earth. RBCO can either carboxylate or oxygenate ribulose-1,5-bisphosphate (RUBP) with CO<sub>2</sub> or O<sub>2</sub>, respectively. RBCO from flowering plants consists of eight large subunits and eight small subunits. 2-carboxylarabinitol-1,5-bisphosphate (2-CABP) is an inhibitor of RCBO. Some additional details can be found in [[Ribulose-1,5-bisphosphate carboxylase/oxygenase]]. | ||
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(under construction) | (under construction) | ||
Here is an isolated <scene name='46/463261/Rubisco_lsu_pair/7'>pair of large subunits</scene>. Each subunit has a large C-terminal lobe and a small N-terminal lobe, and the subunits are arranged head-to-toe (antiparallel) in the pair. <scene name='46/463261/Rubisco_lsu_pair/5'>Two active sites</scene> are located in the interface of the large subunit pair. The subunits are shown in cartoon with one shown in the secondary structure color scheme. Each active site is occupied by RUBP, which is shown in CPK spacefill. Here is a <scene name='46/463261/Rubisco_lsu_monomer/1'>single large subunit</scene> showing that both lobes contain alpha helices (pink) and beta strands (yellow). The large lobe is dominated by an <scene name='46/463261/Rubisco_lsu_monomer/2'>α-β barrel</scene>, which contributes most of the residues in the active | Here is an isolated <scene name='46/463261/Rubisco_lsu_pair/7'>pair of large subunits</scene>. Each subunit has a large C-terminal lobe and a small N-terminal lobe, and the subunits are arranged head-to-toe (antiparallel) in the pair. <scene name='46/463261/Rubisco_lsu_pair/5'>Two active sites</scene> are located in the interface of the large subunit pair. The subunits are shown in cartoon with one shown in the secondary structure color scheme. Each active site is occupied by RUBP, which is shown in CPK spacefill. Here is a <scene name='46/463261/Rubisco_lsu_monomer/1'>single large subunit</scene> showing that both lobes contain alpha helices (pink) and beta strands (yellow). The large lobe is dominated by an <scene name='46/463261/Rubisco_lsu_monomer/2'>α-β barrel</scene> (amino acids 166-409), which contributes most of the residues that form the the active site. One residue from the N-terminal lobe of the adjacent large subunit <scene name='46/463261/Asn123/1'>Asn 123</scene> completes the active site. This scene shows RUBP in spacefill and CPK in one of the active sites in the dimer. Both subunits are shown in transparent cartoon with the α-β barrel is pink and yellow. Asn 123 from the adjacent subunit is in blue spacefill, and residues 121-129 are shown in blue cartoon. This residue does not contribute to catalysis, and it will not be considered further. | ||
== Active Site Structure == | == Active Site Structure == | ||