1rus
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CRYSTAL STRUCTURE OF THE BINARY COMPLEX OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND ITS PRODUCT, 3-PHOSPHO-D-GLYCERATE
OverviewOverview
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., Branden, 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.
About this StructureAbout this Structure
1RUS is a Single protein structure of sequence from Rhodospirillum rubrum with 3PG as ligand. Active as Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the binary complex of ribulose-1,5-bisphosphate carboxylase and its product, 3-phospho-D-glycerate., Lundqvist T, Schneider G, J Biol Chem. 1989 Mar 5;264(7):3643-6. PMID:2492987
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