RTP and Tus: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 56: | Line 56: | ||
The first crystal structure of the Replicator Terminator Protein (RTP) from ''Bacillus subtilis'' was determined in 1995 by Bussiere ''et al.'' (See figure above) <ref>Bussiere DE, Bastia D, White SW (1995) Crystal structure of the replication terminator protein from ''B. subtilis'' at 2.6 A. ''Cell'' 80(4): 651-60.</ref>. This analysis revealed that RTP is comprised of two identical monomers, each of which binds to DNA to form a homodimer. The separate monomers bind at 30 bp sequences known as the A and B termination (Ter) sites. Both of these sites have inverted 16 bp repeats which overlap at highly conserved TAT trinucleotide sequence. This first structure, which used a symmetric B Ter DNA homologue, suggested that the RTP exists as a symmetric homodimer. The idea that a symmetric protein structure could be responsible for an inherently polar mechanism has resulted in a series of proposed solutions and discoveries regarding the mechanism of replication fork arrest. | The first crystal structure of the Replicator Terminator Protein (RTP) from ''Bacillus subtilis'' was determined in 1995 by Bussiere ''et al.'' (See figure above) <ref>Bussiere DE, Bastia D, White SW (1995) Crystal structure of the replication terminator protein from ''B. subtilis'' at 2.6 A. ''Cell'' 80(4): 651-60.</ref>. This analysis revealed that RTP is comprised of two identical monomers, each of which binds to DNA to form a homodimer. The separate monomers bind at 30 bp sequences known as the A and B termination (Ter) sites. Both of these sites have inverted 16 bp repeats which overlap at highly conserved TAT trinucleotide sequence. This first structure, which used a symmetric B Ter DNA homologue, suggested that the RTP exists as a symmetric homodimer. The idea that a symmetric protein structure could be responsible for an inherently polar mechanism has resulted in a series of proposed solutions and discoveries regarding the mechanism of replication fork arrest. | ||
<scene name='RTP_and_Tus/Practice_structure/3'>Secondary Structure</scene> | |||
'''Induced Conformational Change''' | '''Induced Conformational Change''' | ||