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.  RBCO carboxylates or oxygenates ribulose-1,5-bisphosphate (RUBP) with CO<sub>2</sub> or O<sub>2</sub>, respectively.  RBCO from flowering plants usually consists of eight large subunits and eight  small subunits.  2-carboxylarabinitol-1,5-bisphosphate (2-CABP) is an inhibitor of RCBO.  Some additional details in [[Ribulose-1,5-bisphosphate carboxylase/oxygenase]].
'''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 usually 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 sites is occupied by RUBP, which is shown in CPK spacefill. Both lobes of the large subunit contain alpha helices (pink) and beta strands (yellow).  
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 site.  


== Active Site Structure ==
== Active Site Structure ==
(under construction)
(under construction)


The active site is formed by an α-β barrel, which comprises the C-terminal lobe of the large subunit,  and some residues contributed by the N-terminal lobe of the adjacent subunit.  Here is an <scene name='46/463261/Rubisco_lsu_pair/5'>isolated pair of subunits</scene>, , and here is the α-β barrel of that subunit.  
The active site is formed by an α-β barrel, which comprises the C-terminal lobe of the large subunit. Some additional residues are contributed by the N-terminal lobe of the adjacent subunit.  Here is an <scene name='46/463261/Rubisco_lsu_pair/5'>isolated pair of subunits</scene>, , and here is the α-β barrel of that subunit.  




Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alice Harmon, Joel L. Sussman, Alexander Berchansky