Arginine repressor: Difference between revisions
Michal Harel (talk | contribs) New page: <StructureSection load='3laj' size='350' side='right' caption='Structure of arginine repressor complex with DNA and arginine (PDB entry 3laj)' scene=''> '''Arginine repressor''' (A... |
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<StructureSection load='1xxb' size='350' side='right' caption='E. coli structure of arginine repressor C terminal hexamer complex with arginine (PDB entry [[1xxb]])' scene='55/554907/Cv/1'> | |||
== Function == | |||
'''Arginine repressor''' (ArgR) is a prokaryotic repressor which regulates the arginine deiminase pathway. In this pathway, arginine is metabolized to form ammonia, CO2 and ATP. The ArgR releases the expression of the arginine deiminase pathway in the presence of arginine. The genes controlled by ArgR are not found in a single operon. While repressors are usually active as dimers, ArgR is a hexamer and binds to 2 palindromic DNA sites | '''Arginine repressor''' (ArgR) is a prokaryotic repressor which regulates the arginine deiminase pathway. In this pathway, arginine is metabolized to form ammonia, CO2 and ATP. The ArgR releases the expression of the arginine deiminase pathway in the presence of arginine. The genes controlled by ArgR are not found in a single operon. While repressors are usually active as dimers, ArgR is a hexamer and binds to 2 palindromic DNA sites called ARG box in its N terminal domain.<ref>PMID:10331868</ref> | ||
== | == Structural highlights == | ||
The structure of ArgR shows a DNA-binding domain at the acidic N-terminal and a basic C-terminal domain which contains the <scene name='55/554907/Cv/5'>intersubunit interaction sites</scene> and the <scene name='55/554907/Cv/10'>Arg binding site</scene>. Every Arg ligand interacts <scene name='55/554907/Cv/11'>with residues from 3 subunits</scene>.<ref>PMID:8594204</ref> | |||
==3D structures of arginine repressor== | |||
[[Arginine repressor 3D structures]] | |||
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</StructureSection> | |||
== References == | |||
<references/> | |||
[[Category:Topic Page]] | |||
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