1BWV

Activated Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase (RUBISCO) Complexed with the Reaction Intermediate Analogue 2-Carboxyarabinitol 1,5-Bisphosphate

Summary for 1BWV

• Entry DOI: 10.2210/pdb1bwv/pdb
• Descriptor: PROTEIN (RIBULOSE BISPHOSPHATE CARBOXYLASE), MAGNESIUM ION, 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: carbon dioxide fixation, complex (rubisco-reaction intermediate), high specificity factor, lyase
• Biological source: Galdieria partita; More
• Cellular location: Plastid, chloroplast (By similarity): O98949
• Total number of polymer chains: 8
• Total formula weight: 286646.37

Authors

Sugawara, H.,Yamamoto, H.,Shibata, N.,Inoue, T.,Miyake, C.,Yokota, A.,Kai, Y. (deposition date: 1998-09-29, release date: 1999-09-27, Last modification date: 2023-11-15)

Primary citation

Sugawara, H.,Yamamoto, H.,Shibata, N.,Inoue, T.,Okada, S.,Miyake, C.,Yokota, A.,Kai, Y.
Crystal structure of carboxylase reaction-oriented ribulose 1, 5-bisphosphate carboxylase/oxygenase from a thermophilic red alga, Galdieria partita.
J.Biol.Chem., 274:15655-15661, 1999

PubMed Abstract: Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco, EC 4.1.1. 39) obtained from a thermophilic red alga Galdieria partita has the highest specificity factor of 238 among the Rubiscos hitherto reported. Crystal structure of activated Rubisco from G. partita complexed with the reaction intermediate analogue, 2-carboxyarabinitol 1,5-bisphosphate (2-CABP) has been determined at 2.4-A resolution. Compared with other Rubiscos, different amino residues bring the structural differences in active site, which are marked around the binding sites of P-2 phosphate of 2-CABP. Especially, side chains of His-327 and Arg-295 show the significant differences from those of spinach Rubisco. Moreover, the side chains of Asn-123 and His-294 which are reported to bind the substrate, ribulose 1,5-bisphosphate, form hydrogen bonds characteristic of Galdieria Rubisco. Small subunits of Galdieria Rubisco have more than 30 extra amino acid residues on the C terminus, which make up a hairpin-loop structure to form many interactions with the neighboring small subunits. When the structures of Galdieria and spinach Rubiscos are superimposed, the hairpin region of the neighboring small subunit in Galdieria enzyme and apical portion of insertion residues 52-63 characteristic of small subunits in higher plant enzymes are almost overlapped to each other.

PubMed: 10336462
DOI: 10.1074/jbc.274.22.15655

Experimental method

X-RAY DIFFRACTION (2.4 Å)