Welcome! Click here to login or here to register.
 |
|||||||||||||||||||
|
|||||||||||||||||||
 |
|||||||||||||||||||
"Three-dimensional structure of the free radical protein of ribonucleotide reductase." |
Nordlund P, Sjoberg BM, Eklund H |
Published June 14, 1990 in Nature volume 345 .
Pubmed ID: 2190093
Abstract:
| The enzyme ribonucleotide reductase furnishes precursors for the DNA synthesis of all living cells. One of its constituents, the free radical protein, has an unusual alpha-helical structure. There are two iron centres that are about 25 A apart in the dimeric molecule. Tyrosine 122, which harbours the stable free radical necessary for the activity of ribonucleotide reductase, is buried inside the protein and is located 5 A from the closest iron atom. |
This publication refers to following REPAIRtoire entries:
Last modification of this entry: Oct. 11, 2010
Add your own comment!
There is no comment yet.
|
|
|
|