First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.

1uw9

From Proteopedia

Jump to: navigation, search


1uw9, resolution 2.05Å ()
Ligands: , ,
Non-Standard Residues: , ,
Activity: Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39
Related: 1gk8, 1ir2, 1uwa
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

L290F-A222T CHLAMYDOMONAS RUBISCO MUTANT

Publication Abstract from PubMed

Substitution of Leu290 by Phe (L290F) in the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase from the unicellular green alga Chlamydomonas reinhardtii causes a 13% decrease in CO(2)/O(2) specificity and reduced thermal stability. Genetic selection for restored photosynthesis at the restrictive temperature identified an Ala222 to Thr (A222T) substitution that suppresses the deleterious effects of the original mutant substitution to produce a revertant enzyme with improved thermal stability and kinetic properties virtually indistinguishable from that of the wild-type enzyme. Because the mutated residues are situated approximately 19 A away from the active site, they must affect the relative rates of carboxylation and oxygenation in an indirect way. As a means for elucidating the role of such distant interactions in Rubisco catalysis and stability, we have determined the crystal structures of the L290F mutant and L290F/A222T revertant enzymes to 2.30 and 2.05 A resolution, respectively. Inspection of the structures reveals that the mutant residues interact via van der Waals contacts within the same large subunit (intrasubunit path, 15.2 A Calpha-Calpha) and also via a path involving a neighboring small subunit (intersubunit path, 18.7 A Calpha-Calpha). Structural analysis of the mutant enzymes identified regions (residues 50-72 of the small subunit and residues 161-164 and 259-264 of the large subunit) that show significant and systematically increased atomic temperature factors in the L290F mutant enzyme compared to wild type. These regions coincide with residues on the interaction paths between the L290F mutant and A222T suppressor sites and could explain the temperature-conditional phenotype of the L290F mutant strain. This suggests that alterations in subunit interactions will influence protein dynamics and, thereby, affect catalysis.

Altered intersubunit interactions in crystal structures of catalytically compromised ribulose-1,5-bisphosphate carboxylase/oxygenase., Karkehabadi S, Taylor TC, Spreitzer RJ, Andersson I, Biochemistry. 2005 Jan 11;44(1):113-20. PMID:15628851

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1uw9 is a 16 chain structure with sequence from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA.

See Also

Reference

  • Karkehabadi S, Taylor TC, Spreitzer RJ, Andersson I. Altered intersubunit interactions in crystal structures of catalytically compromised ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry. 2005 Jan 11;44(1):113-20. PMID:15628851 doi:http://dx.doi.org/10.1021/bi047928e

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools