Rop protein: Difference between revisions

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{{STRUCTURE_1rop| PDB=1rop  | SIZE=400| SCENE= |right|CAPTION=E. coli Rop protein [[1rop]].}}
{{STRUCTURE_1rop| PDB=1rop  | SIZE=400| SCENE= |right|CAPTION=E. coli Rop protein [[1rop]].}}
 
==Function==
<scene name='Rop_protein/Wt_rop/1'>Rop</scene> '''(Repressor Of Primer)''' is a small homodimeric RNA-binding protein that is involved in the regulation of copy number of the ColE1 plasmids of E.coli, where it is encoded<ref>pmid 2462471</ref>. Its structure has been studied using both X-ray crystallography<ref>PMID:3681971</ref> and NMR<ref>PMID:1841691</ref>.  
<scene name='Rop_protein/Wt_rop/1'>Rop</scene> '''(Repressor Of Primer)''' is a small homodimeric RNA-binding protein that is involved in the regulation of copy number of the ColE1 plasmids of E.coli, where it is encoded<ref>pmid 2462471</ref>. Its structure has been studied using both X-ray crystallography<ref>PMID:3681971</ref> and NMR<ref>PMID:1841691</ref>.  
Each monomer has molecular weight of about 7.500 Da and it consists of 63 amino acids that form two α-helices connected by <scene name='Rop_protein/Wt_rop_loop/2'> a loop </scene>of four amino acids (L29, D30, A31, D32). The two monomers are related with a 2-fold symmetry axis.  
Each monomer has molecular weight of about 7.500 Da and it consists of 63 amino acids that form two α-helices connected by <scene name='Rop_protein/Wt_rop_loop/2'> a loop </scene>of four amino acids (L29, D30, A31, D32). The two monomers are related with a 2-fold symmetry axis.  

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Student, Maria Amprazi, Nicole R Pendini, Keith Callenberg, David Canner, Jaime Prilusky, Michal Harel, Alexander Berchansky