1RUS

CRYSTAL STRUCTURE OF THE BINARY COMPLEX OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND ITS PRODUCT, 3-PHOSPHO-D-GLYCERATE

Summary for 1RUS

• Entry DOI: 10.2210/pdb1rus/pdb
• Descriptor: RUBISCO (RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE), 3-PHOSPHOGLYCERIC ACID (2 entities in total)
• Functional Keywords: lyase(carbon-carbon)
• Biological source: Rhodospirillum rubrum
• Total number of polymer chains: 2
• Total formula weight: 106909.86

Authors

Lundqvist, T.,Schneider, G. (deposition date: 1991-10-10, release date: 1991-10-15, Last modification date: 2024-02-14)

Primary citation

Lundqvist, T.,Schneider, G.
Crystal structure of the binary complex of ribulose-1,5-bisphosphate carboxylase and its product, 3-phospho-D-glycerate.
J.Biol.Chem., 264:3643-3646, 1989

PubMed Abstract: The crystal structure of the binary complex of non-activated ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum and its product 3-phospho-D-glycerate has been determined to 2.9-A resolution. This structure determination confirms the proposed location of the active site (Schneider, G., Lindqvist, Y., Brändén, C.-I., and Lorimer, G. (1986) EMBO J. 5, 3409-3415) at the carboxyl end of the beta-strands of the alpha/beta-barrel in the carboxyl-terminal domain. One molecule of 3-phosphoglycerate is bound per active site. All oxygen atoms of 3-phosphoglycerate form hydrogen bonds to groups of the enzyme. The phosphate group interacts with the sidechains of residues Arg-288, His-321, and Ser-368, which are conserved between enzymes from different species as well as with the main chain nitrogens from residues Thr-322 and Gly-323. These amino acid residues constitute one of the two phosphate binding sites of the active site. The carboxyl group interacts with the side chains of His-287, Lys-191, and Asn-111. Implications of the activation process for the binding of 3-phosphoglycerate are discussed.

PubMed: 2492987

Experimental method

X-RAY DIFFRACTION (2.9 Å)