Rop protein: Difference between revisions

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

Revision as of 18:28, 6 June 2008 view source Nicole R Pendini (talk \| contribs) 31 edits No edit summary ← Older edit		Revision as of 18:29, 6 June 2008 view source Nicole R Pendini (talk \| contribs) 31 edits No edit summary Newer edit →
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	{{STRUCTURE_1rop \| PDB=1rop \| SCENE=Rop_protein/Wt_rop/1}}<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>[Polisky], 1988</ref>. Its structure has been studied using both X-ray crystallography (Banner ''et al.'', 1987) and NMR (Eberle ''et al''., 1991).		{{STRUCTURE_1rop \| PDB=1rop \| SCENE=Rop_protein/Wt_rop/1}}<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>[[Polisky]], 1988</ref>. Its structure has been studied using both X-ray crystallography (Banner ''et al.'', 1987) and NMR (Eberle ''et al''., 1991).
	Each monomer has molecular weight of 14456 Da and it is consisted of 63 amino acids that forms 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 14456 Da and it is consisted of 63 amino acids that forms 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.