Update radar.md

#187 (closed) Experimental Structures should be added https://www.sciencedirect.com/science/article/pii/S0092867423000429 https://www.sciencedirect.com/science/article/pii/S0092867423000569

content/3.defense-systems/radar.md

@@ -9,17 +9,25 @@ tableColumns:
     Sensor: Unknown
     Activator: Unknown
     Effector: Nucleic acid degrading
+
+contributors: 
+  - Hugo Vaysset
+  - Aude Bernheim
+relevantAbstracts:
+  - doi: 10.1016/j.cell.2023.01.026
+  - doi: 10.1016/j.cell.2023.01.012
+  - doi: 10.1126/science.aba0372
 ---
 
 # RADAR
 ## Description
 
-RADAR is comprised of two genes, encoding respectively for an adenosine triphosphatase (RdrA) and  a divergent adenosine deaminase (RdrB) (1), which are in some cases associated with a small membrane protein (RdrC or D) (1). 
-
-RADAR was found to perform RNA editing of adenosine to inosine during phage infection. Editing sites are broadly distributed on the host transcriptome, which could prove deleterious to the host and explain the observed growth arrest of RADAR upon phage infection.  
+RADAR (Restriction by an Adenosine Deaminase Acting on RNA) is comprised of two genes, encoding respectively for an adenosine triphosphatase (RdrA) and  a divergent adenosine deaminase (RdrB), which are in some cases associated with a small membrane protein (RdrC or D). They were first uncovered in a study exploring content of defense islands :ref{doi=10.1126/science.aba0372}. 
 
 ## Molecular mechanism
-RADAR mediates growth arrest upon infection and is therefore considered to be an Abortive infection system.
+In the initial study describing RADAR, RADAR was found to perform RNA editing of adenosine to inosine during phage infection :ref{doi=10.1126/science.aba0372}. Editing sites were broadly distributed on the host transcriptome, which could prove deleterious leading to observed growth arrest of RADAR upon phage infection.  
+Further structural studies revealed potential different mechanism of actions :ref{doi=10.1016/j.cell.2023.01.026,10.1016/j.cell.2023.01.012}. RdrA and RdrB assemble to form a giant 10 MDa complex. The RADAR defense system limits phage replication by catalyzing ATP deamination. Within this system, RdrB functions as an adenosine deaminase, leading to the buildup of ITP (Inosine Tri-Phosphate) and dITP. RdrA induces RdrB activity and potentially regulates the detection of phage infections.
+
 
 ## Example of genomic structure
 
@@ -48,6 +56,86 @@ Proportion of genome encoding the RADAR system for the 14 phyla with more than 5
 
 ## Structure
 
+### Experimentaly determined structure
+
+From :ref{doi=10.1016/j.cell.2023.01.012} in *Escherichia coli*:
+
+::molstar-pdbe-plugin
+---
+height: 700
+dataUrl: /radar/8fnt_EcRdrA_7mer.pdb
+---
+::
+
+
+::molstar-pdbe-plugin
+---
+height: 700
+dataUrl: /radar/8fnv_EcRdrB_12mer.pdb
+---
+::
+
+
+::molstar-pdbe-plugin
+---
+height: 700
+dataUrl: /radar/8fnw_EcRdrAB_7_12mer.cif
+---
+::
+
+From :ref{doi=10.1016/j.cell.2023.01.012} in *Streptococcus suis*:
+
+::molstar-pdbe-plugin
+---
+height: 700
+dataUrl: /radar/8fnu_SsRdrA_7mer.pdb
+---
+::
+
+From :ref{doi=10.1016/j.cell.2023.01.026} in *Escherichia coli*:
+
+::molstar-pdbe-plugin
+---
+height: 700
+dataUrl: /radar/8hr8_EcRdrA_7mer.pdb
+---
+::
+
+::molstar-pdbe-plugin
+---
+height: 700
+dataUrl: /radar/8hr9_EcRdrA_14mer.pdb
+---
+::
+
+::molstar-pdbe-plugin
+---
+height: 700
+dataUrl: /radar/8hrc_EcRdrB_12mer.pdb
+---
+::
+
+::molstar-pdbe-plugin
+---
+height: 700
+dataUrl: /radar/8hr7_EcRdrAB_7_12mer.cif
+---
+::
+
+::molstar-pdbe-plugin
+---
+height: 700
+dataUrl: /radar/8hra_EcRdrA_7mer_rna.pdb
+---
+::
+
+::molstar-pdbe-plugin
+---
+height: 700
+dataUrl: /radar/8hrb_EcRdrA_14mer_rna.pdb
+---
+::
+
 ### radar_I
 
 ::molstar-pdbe-plugin
@@ -143,17 +231,3 @@ end
     style Title3 fill:none,stroke:none,stroke-width:none
     style Title4 fill:none,stroke:none,stroke-width:none
 </mermaid>
-## Relevant abstracts
-
-::relevant-abstracts
----
-items:
-    - doi: 10.1126/science.aba0372
-
----
-::
-
-
-## References
-
-1. Gao L, Altae-Tran H, Böhning F, et al. Diverse enzymatic activities mediate antiviral immunity in prokaryotes. *Science*. 2020;369(6507):1077-1084. doi:10.1126/science.aba0372