4B27

Trp RNA-binding attenuation protein: modifying symmetry and stability of a circular oligomer

Summary for 4B27

• Entry DOI: 10.2210/pdb4b27/pdb
• Related: 1WAP 3ZZQ
• Descriptor: TRANSCRIPTION ATTENUATION PROTEIN MTRB, TRYPTOPHAN (3 entities in total)
• Functional Keywords: transcription, transcription regulation, thermofluor, protein engineering
• Biological source: BACILLUS SUBTILIS
• Total number of polymer chains: 6
• Total formula weight: 51448.38

Authors

Bayfield, O.W.,Chen, C.,Patterson, A.R.,Luan, W.,Smits, C.,Gollnick, P.,Antson, A.A. (deposition date: 2012-07-12, release date: 2012-09-19, Last modification date: 2023-12-20)

Primary citation

Bayfield, O.W.,Chen, C.,Patterson, A.R.,Luan, W.,Smits, C.,Gollnick, P.,Antson, A.A.
Trp RNA-Binding Attenuation Protein: Modifying Symmetry and Stability of a Circular Oligomer.
Plos One, 7:44309-, 2012

PubMed Abstract: Subunit number is amongst the most important structural parameters that determine size, symmetry and geometry of a circular protein oligomer. The L-tryptophan biosynthesis regulator, TRAP, present in several Bacilli, is a good model system for investigating determinants of the oligomeric state. A short segment of C-terminal residues defines whether TRAP forms an 11-mer or 12-mer assembly. To understand which oligomeric state is more stable, we examine the stability of several wild type and mutant TRAP proteins.

PubMed: 22970197
DOI: 10.1371/JOURNAL.PONE.0044309

Experimental method

X-RAY DIFFRACTION (2.72 Å)