2v69

From Proteopedia

Revision as of 15:38, 30 October 2007

CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII RUBISCO WITH A LARGE-SUBUNIT MUTATION D473E

Overview

The loop between alpha-helix 6 and beta-strand 6 in the alpha/beta-barrel, of ribulose-1,5-bisphosphate carboxylase/oxygenase plays a key role in, discriminating between CO2 and O2. Genetic screening in Chlamydomonas, reinhardtii previously identified a loop-6 V331A substitution that, decreases carboxylation and CO2/O2 specificity. Revertant selection, identified T342I and G344S substitutions that restore photosynthetic, growth by increasing carboxylation and specificity of the V331A enzyme. In, numerous X-ray crystal structures, loop 6 is closed or open depending on, the activation state of the enzyme and the presence or absence of ligands., The carboxy terminus folds over loop 6 in the closed state. To study the, molecular basis for catalysis, directed mutagenesis and chloroplast, ... [(full description)]

About this Structure

2V69 is a [Protein complex] structure of sequences from [Chlamydomonas reinhardtii] with MG, CAP and EDO as [ligands]. Active as [Ribulose-bisphosphate carboxylase], with EC number [4.1.1.39]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structural Analysis of Altered Large-Subunit Loop-6/Carboxy-Terminus Interactions That Influence Catalytic Efficiency and CO(2)/O(2) Specificity of Ribulose-1,5-bisphosphate Carboxylase/Oxygenase(,)., Karkehabadi S, Satagopan S, Taylor TC, Spreitzer RJ, Andersson I, Biochemistry. 2007 Oct 2;46(39):11080-9. Epub 2007 Sep 8. PMID:17824672

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