[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0022-2836(82)90547-2; PubMed=6302265 [NCBI, ExPASy, EBI, Israel, Japan]
Dron M.,
Rahire M.,
Rochaix J.-D.;
"Sequence of the chloroplast DNA region of Chlamydomonas reinhardii containing the gene of the large subunit of ribulose bisphosphate carboxylase and parts of its flanking genes.";
J. Mol. Biol. 162:775-793(1982).
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[2]
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PROTEIN SEQUENCE OF 3-14, AND ACETYLATION AT PRO-3.
PubMed=16668742 [NCBI, ExPASy, EBI, Israel, Japan]
Houtz R.L.,
Poneleit L.,
Jones S.B.,
Royer M.,
Stults J.T.;
"Posttranslational modifications in the amino-terminal region of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase from several plant species.";
Plant Physiol. 98:1170-1174(1992).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1105/tpc.006155; PubMed=12417694 [NCBI, ExPASy, EBI, Israel, Japan]
Maul J.E.,
Lilly J.W.,
Cui L.,
dePamphilis C.W.,
Miller W.,
Harris E.H.,
Stern D.B.;
"The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a sea of repeats.";
Plant Cell 14:2659-2679(2002).
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[4]
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X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH THE TRANSITION-STATE ANALOG 2-CABP.
STRAIN=2137;
DOI=10.1074/jbc.M107765200; PubMed=11641402 [NCBI, ExPASy, EBI, Israel, Japan]
Taylor T.C.,
Backlund A.,
Bjorhall K.,
Spreitzer R.J.,
Andersson I.;
"First crystal structure of Rubisco from a green alga, Chlamydomonas reinhardtii.";
J. Biol. Chem. 276:48159-48164(2001).
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[5]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH THE TRANSITION-STATE ANALOG 2-CABP.
STRAIN=137c / CC-125;
DOI=10.1006/jmbi.2001.5381; PubMed=11866526 [NCBI, ExPASy, EBI, Israel, Japan]
Mizohata E.,
Matsumura H.,
Okano Y.,
Kumei M.,
Takuma H.,
Onodera J.,
Kato K.,
Shibata N.,
Inoue T.,
Yokota A.,
Kai Y.;
"Crystal structure of activated ribulose-1,5-bisphosphate carboxylase/oxygenase from green alga Chlamydomonas reinhardtii complexed with 2-carboxyarabinitol-1,5-bisphosphate.";
J. Mol. Biol. 316:679-691(2002).
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- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.
- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.
- COFACTOR: Binds 1 magnesium ion per subunit.
- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers.
- SUBCELLULAR LOCATION: Plastid, chloroplast.
- PTM: The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bond reported in 1IR2 may be the result of oxidation during crystallization.
- PTM: The electron density found in the position of Thr-471 (PubMed:11866526 only) suggests it is either O-methylthreonine, or Ile, which may be produced by RNA editing.
- MISCELLANEOUS: The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric "cap" on each end of the "barrel".
- SIMILARITY: Belongs to the RuBisCO large chain family. Type I subfamily.
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