1geh: Difference between revisions

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[[Image:1geh.jpg|left|200px]]
[[Image:1geh.jpg|left|200px]]


{{Structure
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The line below this paragraph, containing "STRUCTURE_1geh", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[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] </span>
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{{STRUCTURE_1geh| PDB=1geh  | SCENE= }}  
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1geh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1geh OCA], [http://www.ebi.ac.uk/pdbsum/1geh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1geh RCSB]</span>
}}


'''CRYSTAL STRUCTURE OF ARCHAEAL RUBISCO (RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE)'''
'''CRYSTAL STRUCTURE OF ARCHAEAL RUBISCO (RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE)'''
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[[Category: Maeda, N.]]
[[Category: Maeda, N.]]
[[Category: Miki, K.]]
[[Category: Miki, K.]]
[[Category: pentagonal toroid decamer]]
[[Category: Pentagonal toroid decamer]]
[[Category: rubisco]]
[[Category: Rubisco]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:28:23 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:42:21 2008''

Revision as of 17:28, 2 May 2008

File:1geh.jpg

Template:STRUCTURE 1geh

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 Page seeded by OCA on Fri May 2 17:28:23 2008

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