User:Jakob Raphael Käppler/Sandbox218

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[[Image:Calvin cycle en wikipedia.giv.png|300px|left|thumb|Overview of the calvin cycle <ref>[http://en.wikipedia.org/wiki/File:Calvin-cycle4.svg Image of the Calvin cycle]was obtained from Wikipedia</ref>]]
[[Image:Calvin cycle en wikipedia.giv.png|300px|left|thumb|Overview of the calvin cycle <ref>[http://en.wikipedia.org/wiki/File:Calvin-cycle4.svg Image of the Calvin cycle]was obtained from Wikipedia</ref>]]
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'''Rubisco''' ('''Ribulose-1,5-bisphosphate carboxylase oxygenase''') EC 4.1.1.39, quite likely the most occurring enzyme of the world[1], is found also in plants and bacteria. It simplifies the first step in the Calvin-Benson-bassham-cycle: the catalytic binding of inorganic carbon dioxide to Ribulose-1,5-bisphosphate by a condensation reaction. The enzyme a hexadecamer with the molecular mass 550 kDa, consists out of 16 subunits (L8S8) which are divided into 8 large 50 – 55 kDa units and 8 small 12 – 18 kDa units. The genes which encode for the large subunits are located in the chloroplast whereas the genes for the small subunits are located in the nucleus.
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'''Rubisco''' ('''Ribulose-1,5-bisphosphate carboxylase oxygenase''') EC 4.1.1.39, quite likely the most frequently found enzyme of the world[1], appears in plants as well as bacteria. It simplifies the first step in the Calvin-Benson-bassham-cycle by a condensation reaction, where inorganic carbon dioxide binds in catalysis to Ribulose-1,5-bisphosphate. The enzyme, a hexadecamer with the molecular mass of 550 kDa, consists of 16 subunits (L8S8) which are divided into 8 large 50 – 55 kDa subunits and 8 small 12 – 18 kDa subunits. The genes which encode for the large subunits are located in the chloroplast whereas the genes for the small subunits are located in the nucleus. Rubisco not only catalyze the carbon fixation, it also has an oxygenase reaction. These two reactions are in competition to each other.
==Biological role==
==Biological role==

Revision as of 15:06, 2 January 2012


Spinach Ribulose-1,5-Bisphosphat Carboxylase Oxygenase, 1aus
Spinach Ribulose-1,5-Bisphosphat Carboxylase Oxygenase, 1aus


PDB ID 1rcx

Drag the structure with the mouse to rotate
Crystal structure of spinach RUBISCO in complex with its substrate Ribulose-1,5-bisphosphate 1rcx
Ligands:
Activity: Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml


Overview of the calvin cycle
Overview of the calvin cycle [1]

Rubisco (Ribulose-1,5-bisphosphate carboxylase oxygenase) EC 4.1.1.39, quite likely the most frequently found enzyme of the world[1], appears in plants as well as bacteria. It simplifies the first step in the Calvin-Benson-bassham-cycle by a condensation reaction, where inorganic carbon dioxide binds in catalysis to Ribulose-1,5-bisphosphate. The enzyme, a hexadecamer with the molecular mass of 550 kDa, consists of 16 subunits (L8S8) which are divided into 8 large 50 – 55 kDa subunits and 8 small 12 – 18 kDa subunits. The genes which encode for the large subunits are located in the chloroplast whereas the genes for the small subunits are located in the nucleus. Rubisco not only catalyze the carbon fixation, it also has an oxygenase reaction. These two reactions are in competition to each other.

Contents

Biological role

General structure

detailed structure

3D Structures of RuBisCO

Updated December 2011

RuBisCO

3rg6 – RBCO – Synechococcus elongatus
3qfw - RBCO large subunit – Rhodopseudomonas palustris
1uzh, 1gk8 – CrRBCO – Chlamydomonas reinhardtii
1uw9, 1uwa – CrRBCO (mutant)
1svd – RBCD – Halothiobacillus neapolitanus
1bxn – RBCO – Cupriavidus necator
1aus - spRBCO – spinach
1rba - RrRBCO (mutant) – Rhododpirillum rubrum
5rub - RrRBCO
2wvw – RBCO – Anabena – Cryo EM
2vdh, 2vdi, 2v67, 2v68, 2v63, 2v69, 2v6a - CrRBCO (mutant)
1mlv - pRBCO LSMT – pea
2cxe, 2cwx – PhRBCO - Pyrococcus horikoshii
1uzd – CrRBCO/spRBCO
1geh – TkRBCO – Thermococcus kodakaraensis
1iwa - GpRBCO – Galdieria partita
1tel – RBCO large subunit – Chlorobium tepidum

RuBisCO complex with inhibitor 2-CABP

3kdn, 3a12 – TkRBCO III + 2-CABP
3kdo, 3a13 - TkRBCO III (mutant) + 2-CABP
1ir2 - CrRBCO + 2-CABP
1upm, 1upp, 1rbo, 3ruc, 8ruc - spRBCO + 2-CABP + Cation
1ir1 - spRBCO + 2-CABP + CO2 + Mg
1wdd – RBCO + 2-CABP – rice
1bwv - GpRBCO + 2-CABP

RuBisCO complex with product

1aa1 – spRBCO + phosphoglycerate
1rus - RrRBCO + phosphoglycerate

RuBisCO complex with substrate

1rcx, 1rxo – spRBCO + ribulose-1,5-bisphosphate

RuBisCO complexes

2h21 – pRBCO LSMT + AdoMet
2h23 - pRBCO LSMT + AdoHcy
2h2e, 1ozv, 1p0y - pRBCO LSMT + AdoMet + lysine
2h2j - pRBCO LSMT + sinefungin
2d69 – PhRBCO + sulfate
1rco - spRBCO + xylulose-diol-1,5-bisphosphate
2rus - RrRBCO + CO2 + Mg
1ej7 – RBCO + phosphate - tobacco

Notes and Literarture References

  1. ↑ Image of the Calvin cyclewas obtained from Wikipedia

Proteopedia Page Contributors and Editors

Nicolai Rügen and Jakob Raphael Käppler

Proteopedia Page Contributors and Editors (what is this?)

Jakob Raphael Käppler

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