Nucleotide sequence of the ribulosebisphosphate carboxylase gene from Rhodospirillum rubrum.Nargang F., McIntosh L., Somerville C.R.Cited forNUCLEOTIDE SEQUENCE [GENOMIC DNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)Mol. Gen. Genet. 193:220-224 (1984)Cited in1
Isolation and sequencing of an active-site peptide from Rhodospirillum rubrum ribulosebisphosphate carboxylase/oxygenase after affinity labeling with 2-[(bromoacetyl)amino]pentitol 1,5-bisphosphate.Fraij B., Hartman F.C.View abstractCited forPROTEIN SEQUENCE OF 314-337CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiochemistry 22:1515-1520 (1983)Cited in1
Three-dimensional structure of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at 2.9-A resolution.Schneider G., Lindqvist Y., Braenden C.-I., Lorimer G.View abstractCited forX-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), SUBUNITCategoriesInteraction, StructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCEMBO J. 5:3409-3415 (1986)Cited in1
Crystal structure of the active site of ribulose-bisphosphate carboxylase.Andersson I., Knight S., Schneider G., Lindqvist Y., Lundqvist T., Braenden C.-I., Lorimer G.H.Cited forX-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), COFACTOR, SUBUNITCategoriesFunction, Interaction, StructureSourceUniProtKB reviewed (Swiss-Prot)Nature 337:229-234 (1989)Cited in1
Crystallographic refinement and structure of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum at 1.7-A resolution.Schneider G., Lindqvist Y., Lundqvist T.View abstractCited forX-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), SUBUNITCategoriesInteraction, StructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Mol. Biol. 211:989-1008 (1990)Cited in1
Crystal structure of the ternary complex of ribulose-1,5-bisphosphate carboxylase, Mg(II), and activator CO2 at 2.3-A resolution.Lundqvist T., Schneider G.View abstractCited forX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF ACTIVATED ENZYME, COFACTOR, SUBUNIT, CARBOXYLATION AT LYS-191CategoriesFunction, Interaction, StructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiochemistry 30:904-908 (1991)Cited in1
Substitution of ASP193 to ASN at the active site of ribulose-1,5- bisphosphate carboxylase results in conformational changes.Soderlind E., Schneider G., Gutteridge S.View abstractCited forX-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF MUTANT ASN-193, FUNCTION, ACTIVE SITE, SUBUNIT, MUTAGENESIS OF ASP-193CategoriesFunction, Interaction, Phenotypes & Variants, StructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCEur. J. Biochem. 206:729-735 (1992)Cited in1
Crystal structure of the binary complex of ribulose-1,5-bisphosphate carboxylase and its product, 3-phospho-D-glycerate.Lundqvist T., Schneider G.View abstractCategoriesStructureSourcePDB: 1RUSPubMedEurope PMCJ Biol Chem 264:3643-3646 (1989)Mapped to1
Polypeptide in the chaperonin cage partly protrudes out and then folds inside or escapes outside.Motojima F., Yoshida M.View abstractCategoriesInteractionSourceIntAct: P04718PubMedEurope PMCEMBO J 29:4008-4019 (2010)Mapped to5
Crystal structure of activated ribulose-1,5-bisphosphate carboxylase complexed with its substrate, ribulose-1,5-bisphosphate.Lundqvist T., Schneider G.View abstractCategoriesStructureSourcePDB: 9RUBPubMedEurope PMCJ Biol Chem 266:12604-12611 (1991)Mapped to1