User:Chloe Paul/Replication Terminator Protein: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Chloe Paul (talk | contribs) No edit summary |
Chloe Paul (talk | contribs) No edit summary |
||
| Line 5: | Line 5: | ||
== RTP binding to DNA == | == RTP binding to DNA == | ||
<StructureSection load='1f4k' size='300' side='right' caption='RTP bound to symmetric DNA (PDB entry [[1f4k]])' scene='User:Chloe_Paul/Replication_Terminator_Protein/Rtpsym/1'>RTP has been of interest in terms of its specific binding to DNA because it doesn’t use the common DNA structural motifs such as a basic leucine zipper, zinc finger or helix-turn-helix motif. It has been established that RTP, like Tus, is sequence specific, as it binds as the Ter sites. These comprise two sequences that are imperfect inverted repeats <ref name="bussiere" /><ref name="vivian" />. This means that RTP needs to be able to recognise specific bases in the helical DNA structure by reading the exposed edges of the bases located in the major and minor grooves of DNA. Structurally RTP interacts with DNA through the α3 helices in the major grooves, its anti-parallel β-sheets (β2 and β3) in the minor grooves. The flexible N-terminal regions wrap with non-specific ionic interactions around the DNA <ref name= | <StructureSection load='1f4k' size='300' side='right' caption='RTP bound to symmetric DNA (PDB entry [[1f4k]])' scene='User:Chloe_Paul/Replication_Terminator_Protein/Rtpsym/1'>RTP has been of interest in terms of its specific binding to DNA because it doesn’t use the common DNA structural motifs such as a basic leucine zipper, zinc finger or helix-turn-helix motif. It has been established that RTP, like Tus, is sequence specific, as it binds as the Ter sites. These comprise two sequences that are imperfect inverted repeats <ref name="bussiere" /><ref name="vivian" />. This means that RTP needs to be able to recognise specific bases in the helical DNA structure by reading the exposed edges of the bases located in the major and minor grooves of DNA. Structurally RTP interacts with DNA through the α3 helices in the major grooves, its anti-parallel β-sheets (β2 and β3) in the minor grooves. The flexible N-terminal regions wrap with non-specific ionic interactions around the DNA <ref name="wilce">PMID:11224562</ref>. </StructureSection> | ||
== Symmetric and Asymmetric Conformations == | == Symmetric and Asymmetric Conformations == | ||
