3ZZS
Engineered 12-subunit Bacillus stearothermophilus trp RNA-binding attenuation protein (TRAP)
Summary for 3ZZS
| Entry DOI | 10.2210/pdb3zzs/pdb |
| Related | 1C9S 1GTF 1GTN 1QAW 1UTD 1UTF 1UTV |
| Descriptor | TRANSCRIPTION ATTENUATION PROTEIN MTRB, TRYPTOPHAN (3 entities in total) |
| Functional Keywords | transcription, transcription regulation, protein engineering |
| Biological source | GEOBACILLUS STEAROTHERMOPHILUS |
| Total number of polymer chains | 9 |
| Total formula weight | 66783.79 |
| Authors | Chen, C.,Smits, C.,Dodson, G.G.,Shevtsov, M.B.,Merlino, N.,Gollnick, P.,Antson, A.A. (deposition date: 2011-09-02, release date: 2011-10-12, Last modification date: 2023-12-20) |
| Primary citation | Chen, C.,Smits, C.,Dodson, G.G.,Shevtsov, M.B.,Merlino, N.,Gollnick, P.,Antson, A.A. How to Change the Oligomeric State of a Circular Protein Assembly: Switch from 11-Subunit to 12-Subunit Trap Suggests a General Mechanism Plos One, 6:25296-, 2011 Cited by PubMed Abstract: Many critical cellular functions are performed by multisubunit circular protein oligomers whose internal geometry has evolved to meet functional requirements. The subunit number is arguably the most critical parameter of a circular protein assembly, affecting the internal and external diameters of the assembly and often impacting on the protein's function. Although accurate structural information has been obtained for several circular proteins, a lack of accurate information on alternative oligomeric states has prevented engineering such transitions. In this study we used the bacterial transcription regulator TRAP as a model system to investigate the features that define the oligomeric state of a circular protein and to question how the subunit number could be manipulated. PubMed: 21984911DOI: 10.1371/JOURNAL.PONE.0025296 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.49 Å) |
Structure validation
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