P53R2: Difference between revisions
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m New page: ='''p53R2'''= {{STRUCTURE_3hf1| PDB=3hf1 | SCENE= }} P53R2 is an oxydoreductase composed of 351 residues. It is a small subunit of the ribonucleotide reductase (RNR). RNR catalyses t... |
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=='''Structure and function'''== | =='''Structure and function'''== | ||
The X-ray crystal structure permits to see that p53R2 is made of two monomers A and B themselves made of loops and helix. Two of them play an important role. | The X-ray crystal structure permits to see that p53R2 is made of two monomers A and B themselves made of loops and helix. Two of them play an important role. | ||
<scene name=' | <scene name='Sandbox156/Iron-binding_site/1'>An iron binding site</scene>is highlighted. But concerning this site, the two monomers are not the same. Actually, the B monomer has two iron-binding site (called Fe2 and Fe1) whereas the A monomer has only one which is Fe2. This can be explained by structural changes in the helix that compose the two monomers. The 37 to 42 N-terminal residues (called the swivel loop) from one monomer can rotate between two conformations and can influence the position of the helix B or D on the opposite monomer. | ||
[[Image:Thetwomonomers.jpg|400px]] | [[Image:Thetwomonomers.jpg|400px]] | ||
