2QPE
An unexpected outcome of surface-engineering an integral membrane protein: Improved crystallization of cytochrome ba3 oxidase from Thermus thermophilus
Summary for 2QPE
| Entry DOI | 10.2210/pdb2qpe/pdb |
| Related | 1XME |
| Descriptor | Cytochrome c oxidase subunit 1, Cytochrome c oxidase subunit 2, Cytochrome c oxidase polypeptide 2A, ... (7 entities in total) |
| Functional Keywords | cytochrome ba3 oxidase, heme, integral membrane protein, electron transport, hydrogen ion transport, ion transport, iron, metal-binding, oxidoreductase, respiratory chain, transmembrane, transport, formylation |
| Biological source | Thermus thermophilus More |
| Cellular location | Cell membrane; Multi-pass membrane protein: Q5SJ79 Cell membrane; Single-pass membrane protein: Q5SJ80 P82543 |
| Total number of polymer chains | 3 |
| Total formula weight | 87508.00 |
| Authors | Liu, B.,Luna, V.M.,Chen, Y.,Stout, C.D.,Fee, J.A. (deposition date: 2007-07-23, release date: 2007-12-11, Last modification date: 2023-08-30) |
| Primary citation | Liu, B.,Luna, V.M.,Chen, Y.,Stout, C.D.,Fee, J.A. An unexpected outcome of surface engineering an integral membrane protein: improved crystallization of cytochrome ba(3) from Thermus thermophilus. Acta Crystallogr.,Sect.F, 63:1029-1034, 2007 Cited by PubMed Abstract: Past work has shown that it is feasible to mutate surface residues of soluble proteins and to a lesser extent membrane proteins in order to improve their crystallization behavior. Described here is a successful application of this approach to the integral membrane protein Thermus thermophilus cytochrome ba(3) oxidase. Two mutant forms of this enzyme (I-K258R and I-K258R/II-E4Q) were created in which symmetrical crystal contacts within crystals of wild-type enzyme were modified. These mutant proteins had greatly shortened crystallization times, decreasing from approximately 30 d for the wild type to 1-3 d for the mutants, and crystallization was highly reproducible. Native-like proteins crystallize in space group P4(3)2(1)2, whereas the mutant proteins crystallize in space group P4(1)2(1)2 with a different packing arrangement. Crystals of the P4(3)2(1)2 form occasionally diffracted to 2.4-2.3 A resolution following controlled dehydration, while those of the P4(1)2(1)2 form routinely diffracted to between 3.0 and 2.6 A for crystals that had been cryoprotected but not dehydrated. PubMed: 18084085DOI: 10.1107/S1744309107054176 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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