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| - | [[Image:1uwa.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1uwa| PDB=1uwa | SCENE= }} | | {{STRUCTURE_1uwa| PDB=1uwa | SCENE= }} |
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| - | '''L290F MUTANT RUBISCO FROM CHLAMYDOMONAS'''
| + | ===L290F MUTANT RUBISCO FROM CHLAMYDOMONAS=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15628851}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15628851 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15628851}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Photosynthesis]] | | [[Category: Photosynthesis]] |
| | [[Category: Rubisco]] | | [[Category: Rubisco]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:46:08 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:30:16 2008'' |
Revision as of 09:30, 27 July 2008
Template:STRUCTURE 1uwa
L290F MUTANT RUBISCO FROM CHLAMYDOMONAS
Template:ABSTRACT PUBMED 15628851
About this Structure
1UWA is a Protein complex structure of sequences from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA.
Reference
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
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