User:Jakob Raphael Käppler/Sandbox218

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Crystal Structure of Spinach Ribulose-1,5-bisphosphat Carboxylase Oxygenase in Complex with its Substrate Ribulose-1,5-bisphosphate
Ligands:
Activity:	Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39
Structural annotation: Resources: CATH : 1Rcxb02, 1Rcxb01, 1Rcxc00, 1Rcxe01, 1Rcxe02, 1Rcxf00, 1Rcxh02, 1Rcxh01, 1Rcxi00, 1Rcxk02, 1Rcxk01, 1Rcxl01, 1Rcxl02, 1Rcxm00, 1Rcxo02, 1Rcxo01, 1Rcxp00, 1Rcxr02, 1Rcxr01, 1Rcxs00, 1Rcxt00, 1Rcxv01, 1Rcxv02, 1Rcxw00 InterPro : Ipr000685, Ipr000894 Pfam : PF00016, PF02788, PF00101 SCOP : d1rcxb2, d1rcxb1, d1rcxc_, d1rcxe2, d1rcxe1, d1rcxf_, d1rcxh2, d1rcxh1, d1rcxi_, d1rcxk2, d1rcxk1, d1rcxl2, d1rcxl1, d1rcxm_, d1rcxo2, d1rcxo1, d1rcxp_, d1rcxr1, d1rcxr2, d1rcxs_, d1rcxt_, d1rcxv2, d1rcxv1, d1rcxw_ UniProt : P00875, P00870
Functional annotation: Cellular component: chloroplast chloroplast ribulose bisphosphate carboxylase complex Biological process: carbon utilization by fixation of carbon dioxide photosynthesis photorespiration reductive pentose-phosphate cycle Molecular function: lyase activity magnesium ion binding metal ion binding ribulose-bisphosphate carboxylase activity monooxygenase activity oxidoreductase activity
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, PDBsum, RCSB
Coordinates:	save as pdb, mmCIF, xml

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.

Contents 1 Biological role 2 General structure 2.1 detailed structure 3 3D Structures of RuBisCO 3.1 RuBisCO 3.2 RuBisCO complex with inhibitor 2-CABP 3.3 RuBisCO complex with product 3.4 RuBisCO complex with substrate 3.5 RuBisCO complexes 4 Notes and Literarture References 5 Proteopedia Page Contributors and Editors

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. ↑ [1]from Wikipedia

Proteopedia Page Contributors and Editors

Nicolai Rügen and Jakob Raphael Käppler