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[[Image:1geh.jpg|left|200px]]
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{{STRUCTURE_1geh|  PDB=1geh  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF ARCHAEAL RUBISCO (RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE)'''


==CRYSTAL STRUCTURE OF ARCHAEAL RUBISCO (RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE)==
<StructureSection load='1geh' size='340' side='right'caption='[[1geh]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1geh]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_kodakarensis_KOD1 Thermococcus kodakarensis KOD1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GEH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1geh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1geh OCA], [https://pdbe.org/1geh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1geh RCSB], [https://www.ebi.ac.uk/pdbsum/1geh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1geh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RBL_THEKO RBL_THEKO] Catalyzes the addition of molecular CO(2) and H(2)O to ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3-phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and R15P isomerase.[HAMAP-Rule:MF_01133]<ref>PMID:17303759</ref> <ref>PMID:20926376</ref> <ref>PMID:9988755</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:11435112</ref>
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 Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 1geh" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[RuBisCO 3D structures|RuBisCO 3D structures]]
[[Category: Ribulose-bisphosphate carboxylase]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Thermococcus kodakarensis]]
__TOC__
[[Category: Atomi, H.]]
</StructureSection>
[[Category: Fukui, T.]]
[[Category: Large Structures]]
[[Category: Imanaka, T.]]
[[Category: Thermococcus kodakarensis KOD1]]
[[Category: Kitano, K.]]
[[Category: Atomi H]]
[[Category: Maeda, N.]]
[[Category: Fukui T]]
[[Category: Miki, K.]]
[[Category: Imanaka T]]
[[Category: Pentagonal toroid decamer]]
[[Category: Kitano K]]
[[Category: Rubisco]]
[[Category: Maeda N]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:28:23 2008''
[[Category: Miki K]]
Retrieved from "https://proteopedia.org/1geh"