1gk8
From Proteopedia
|
RUBISCO FROM CHLAMYDOMONAS REINHARDTII
Overview
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.
About this Structure
1GK8 is a Protein complex structure of sequences from Chlamydomonas reinhardtii with , and as ligands. Active as Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
First crystal structure of Rubisco from a green alga, Chlamydomonas reinhardtii., Taylor TC, Backlund A, Bjorhall K, Spreitzer RJ, Andersson I, J Biol Chem. 2001 Dec 21;276(51):48159-64. Epub 2001 Oct 18. PMID:11641402
Page seeded by OCA on Sun Feb 3 09:40:36 2008
