1GK8

Rubisco from Chlamydomonas reinhardtii

Summary for 1GK8

• Entry DOI: 10.2210/pdb1gk8/pdb
• Related: 1AA1 1AUS 1BWV 1BXN 1EJ7 1GK8 1RBA 1RBL 1RBO 1RCO 1RCX 1RLC 1RLD 1RSC 1RUS 1RXO 2RUS 5RUB 8RUC 9RUB
• Descriptor: RIBULOSE-1,5 BISPHOSPHATE CARBOXYLASE LARGE CHAIN, RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: lyase, rubisco, photosynthesis
• Biological source: CHLAMYDOMONAS REINHARDTII; More
• Total number of polymer chains: 8
• Total formula weight: 279492.51

Authors

Taylor, T.C. (deposition date: 2001-08-09, release date: 2001-10-24, Last modification date: 2023-12-13)

Primary citation

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-, 2001

PubMed Abstract: The crystal structure of Rubisco (ribulose 1,5-bisphosphate carboxylase/oxygenase) from the unicellular green alga Chlamydomonas reinhardtii has been determined to 1.4 A resolution. Overall, the structure shows high similarity to the previously determined structures of L8S8 Rubisco enzymes. The largest difference is found in the loop between beta strands A and B of the small subunit (betaA-betaB loop), which is longer by six amino acid residues than the corresponding region in Rubisco from Spinacia. Mutations of residues in the betaA-betaB loop have been shown to affect holoenzyme stability and catalytic properties. The information contained in the Chlamydomonas structure enables a more reliable analysis of the effect of these mutations. No electron density was observed for the last 13 residues of the small subunit, which are assumed to be disordered in the crystal. Because of the high resolution of the data, some posttranslational modifications are unambiguously apparent in the structure. These include cysteine and N-terminal methylations and proline 4-hydroxylations.

PubMed: 11641402
DOI: 10.1074/JBC.M107765200

Experimental method

X-RAY DIFFRACTION (1.4 Å)