1uw9
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(New page: 200px<br /> <applet load="1uw9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uw9, resolution 2.05Å" /> '''L290F-A222T CHLAMYD...)
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Revision as of 14:58, 29 October 2007
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L290F-A222T CHLAMYDOMONAS RUBISCO MUTANT
Overview
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 ... [(full description)]
About this Structure
1UW9 is a [Protein complex] structure of sequences from [Chlamydomonas reinhardtii] with MG, CAP and EDO as [ligands]. Active as [[1]], with EC number [4.1.1.39]. 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
Page seeded by OCA on Mon Oct 29 17:03:38 2007
