Structure of the RuBisCO chaperone RbcX from the thermophilic cyanobacteriumThermosynechococcus elongatus
| Autor: | Miroslaw Tarnawski, Andrzej Szczepaniak, Wojciech Bialek, Mariusz Jaskolski, S. Krzywda |
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| Rok vydání: | 2011 |
| Předmět: |
inorganic chemicals
Models Molecular Ribulose-Bisphosphate Carboxylase Protein subunit Biophysics Cyanobacteria Biochemistry Protein structure Bacterial Proteins Structural Biology Mutant protein Genetics Structural Communications Protein Structure Quaternary Thermophilic organism biology Thermophile fungi RuBisCO food and beverages Hydrogen Bonding Condensed Matter Physics Protein Structure Tertiary Chaperone (protein) biology.protein Protein Multimerization Hydrophobic and Hydrophilic Interactions Molecular Chaperones Cysteine |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67:851-857 |
| ISSN: | 1744-3091 |
| DOI: | 10.1107/s1744309111018860 |
| Popis: | The crystal structure of TeRbcX, a RuBisCO assembly chaperone from the cyanobacterium Thermosynechococcus elongatus, a thermophilic organism, has been determined at 1.7 Å resolution. TeRbcX has an unusual cysteine residue at position 103 that is not found in RbcX proteins from mesophilic organisms. Unlike wild-type TeRbcX, a mutant protein with Cys103 replaced by Ala (TeRbcX-C103A) could be readily crystallized. The structure revealed that the overall fold of the TeRbcX homodimer is similar to those of previously crystallized RbcX proteins. Normal-mode analysis suggested that TeRbcX might adopt an open or closed conformation through a hinge movement pivoted on a kink in two long α4 helices. This type of conformational transition is presumably connected to RbcL (the large RuBisCO subunit) binding during the chaperone function of the RuBisCO assembly. |
| Databáze: | OpenAIRE |
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