1GEH

CRYSTAL STRUCTURE OF ARCHAEAL RUBISCO (RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE)

Summary for 1GEH

Entry DOI	10.2210/pdb1geh/pdb
Descriptor	RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE, SULFATE ION (2 entities in total)
Functional Keywords	pentagonal toroid decamer, rubisco, lyase
Biological source	Thermococcus kodakarensis
Total number of polymer chains	5
Total formula weight	249843.03
Authors	Kitano, K.,Maeda, N.,Fukui, T.,Atomi, H.,Imanaka, T.,Miki, K. (deposition date: 2000-11-13, release date: 2001-12-19, Last modification date: 2023-12-27)
Primary citation	Kitano, K.,Maeda, N.,Fukui, T.,Atomi, H.,Imanaka, T.,Miki, K. Crystal Structure of a Novel-Type Archaeal Rubisco with Pentagonal Symmetry Structure, 9:473-481, 2001 Cited by PubMed Abstract: 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. PubMed: 11435112 DOI: 10.1016/S0969-2126(01)00608-6 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.8 Å)

Structure validation