4P86

Structure of PyrR protein from Bacillus subtilis with GMP

4P86 の概要

• エントリーDOI: 10.2210/pdb4p86/pdb
• 分子名称: Bifunctional protein PyrR, GUANOSINE-5'-MONOPHOSPHATE, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: rna binding proteins, transferase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 84001.00

構造登録者

Perica, T.,Kondo, Y.,Tiwari, S.,McLaughlin, S.,Steward, A.,Reuter, N.,Clarke, J.,Teichmann, S.A. (登録日: 2014-03-30, 公開日: 2014-12-17, 最終更新日: 2023-12-20)

主引用文献

Perica, T.,Kondo, Y.,Tiwari, S.P.,McLaughlin, S.H.,Kemplen, K.R.,Zhang, X.,Steward, A.,Reuter, N.,Clarke, J.,Teichmann, S.A.
Evolution of oligomeric state through allosteric pathways that mimic ligand binding.
Science, 346:1254346-1254346, 2014

PubMed Abstract: Evolution and design of protein complexes are almost always viewed through the lens of amino acid mutations at protein interfaces. We showed previously that residues not involved in the physical interaction between proteins make important contributions to oligomerization by acting indirectly or allosterically. In this work, we sought to investigate the mechanism by which allosteric mutations act, using the example of the PyrR family of pyrimidine operon attenuators. In this family, a perfectly sequence-conserved helix that forms a tetrameric interface is exposed as solvent-accessible surface in dimeric orthologs. This means that mutations must be acting from a distance to destabilize the interface. We identified 11 key mutations controlling oligomeric state, all distant from the interfaces and outside ligand-binding pockets. Finally, we show that the key mutations introduce conformational changes equivalent to the conformational shift between the free versus nucleotide-bound conformations of the proteins.

PubMed: 25525255
DOI: 10.1126/science.1254346

実験手法

X-RAY DIFFRACTION (1.93 Å)