1geh: Difference between revisions
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[[Image:1geh.jpg|left|200px]] | [[Image:1geh.jpg|left|200px]] | ||
'''CRYSTAL STRUCTURE OF ARCHAEAL RUBISCO (RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE)''' | {{Structure | ||
|PDB= 1geh |SIZE=350|CAPTION= <scene name='initialview01'>1geh</scene>, resolution 2.8Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF ARCHAEAL RUBISCO (RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1GEH is a [ | 1GEH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermococcus_kodakarensis Thermococcus kodakarensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GEH OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of a novel-type archaeal rubisco with pentagonal symmetry., Kitano K, Maeda N, Fukui T, Atomi H, Imanaka T, Miki K, Structure. 2001 Jun;9(6):473-81. PMID:[http:// | Crystal structure of a novel-type archaeal rubisco with pentagonal symmetry., Kitano K, Maeda N, Fukui T, Atomi H, Imanaka T, Miki K, Structure. 2001 Jun;9(6):473-81. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11435112 11435112] | ||
[[Category: Ribulose-bisphosphate carboxylase]] | [[Category: Ribulose-bisphosphate carboxylase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rubisco]] | [[Category: rubisco]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:21:59 2008'' | ||
Revision as of 12:21, 20 March 2008
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| , resolution 2.8Å | |||||||
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| Ligands: | |||||||
| Activity: | Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF ARCHAEAL RUBISCO (RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE)
OverviewOverview
BACKGROUND: Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the key enzyme of the Calvin-Benson cycle and catalyzes the primary reaction of CO2 fixation in plants, algae, and bacteria. Rubiscos have been so far classified into two types. Type I is composed of eight large subunits (L subunits) and eight small subunits (S subunits) with tetragonal symmetry (L8S8), but type II is usually composed only of two L subunits (L2). Recently, some genuinely active Rubiscos of unknown physiological function have been reported from archaea. RESULTS: The crystal structure of Rubisco from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 (Tk-Rubisco) was determined at 2.8 A resolution. The enzyme is composed only of L subunits and showed a novel (L2)5 decameric structure. Compared to previously known type I enzymes, each L2 dimer is inclined approximately 16 degrees to form a toroid-shaped decamer with its unique L2-L2 interfaces. Differential scanning calorimetry (DSC), circular dichroism (CD), and gel permeation chromatography (GPC) showed that Tk-Rubisco maintains its secondary structure and decameric assembly even at high temperatures. CONCLUSIONS: The present study provides the first structure of an archaeal Rubisco, an unprecedented (L2)5 decamer. Biochemical studies indicate that Tk-Rubisco maintains its decameric structure at high temperatures. The structure is distinct from type I and type II Rubiscos and strongly supports that Tk-Rubisco should be classified as a novel type III Rubisco.
About this StructureAbout this Structure
1GEH is a Single protein structure of sequence from Thermococcus kodakarensis. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a novel-type archaeal rubisco with pentagonal symmetry., Kitano K, Maeda N, Fukui T, Atomi H, Imanaka T, Miki K, Structure. 2001 Jun;9(6):473-81. PMID:11435112
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