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First crystal structure of Rubisco from a green alga, Chlamydomonas reinhardtii
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Division of Pharmacognosy.
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2001 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 276, no 51, 48159-48164 p.Article in journal (Refereed) Published
Abstract [en]

The crystal structure of Rubisco (ribulose 1,5-bisphosphate carboxylase/oxygenase) from the unicellular green alga, Chlamydomonas reinhardtii has been determined to 1.4 Angstrom 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.

Place, publisher, year, edition, pages
2001. Vol. 276, no 51, 48159-48164 p.
National Category
Structural Biology
URN: urn:nbn:se:uu:diva-63209DOI: 10.1074/jbc.M107765200PubMedID: 11641402OAI: oai:DiVA.org:uu-63209DiVA: diva2:91120
Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2012-03-22Bibliographically approved

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