Summary for 3Q20
| Entry DOI | 10.2210/pdb3q20/pdb |
| Descriptor | RbcX protein, ACETATE ION, HEXANE-1,6-DIOL, ... (4 entities in total) |
| Functional Keywords | helix bundle, chaperone, rubisco assembly |
| Biological source | Thermosynechococcus elongatus |
| Total number of polymer chains | 2 |
| Total formula weight | 29499.17 |
| Authors | Tarnawski, M.,Krzywda, S.,Szczepaniak, A.,Jaskolski, M. (deposition date: 2010-12-19, release date: 2011-01-26, Last modification date: 2023-11-01) |
| Primary citation | Tarnawski, M.,Krzywda, S.,Bialek, W.,Jaskolski, M.,Szczepaniak, A. Structure of the RuBisCO chaperone RbcX from the thermophilic cyanobacterium Thermosynechococcus elongatus Acta Crystallogr.,Sect.F, 67:851-857, 2011 Cited by PubMed Abstract: 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. PubMed: 21821880DOI: 10.1107/S1744309111018860 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.71 Å) |
Structure validation
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