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| PROSITE documentation PDOC00317 |
Ribonucleotide reductase small subunit signature
Description:
Ribonucleotide reductase (EC 1.17.4.1) [1,2] catalyzes the reductive synthesis
of deoxyribonucleotides from their corresponding ribonucleotides. It provides
the precursors necessary for DNA synthesis. Ribonucleotide reductase is an
oligomeric enzyme composed of a large subunit (700 to 1000 residues) and a
small subunit (300 to 400 residues).
The small chain binds two iron atoms [3] (three Glu, one Asp, and two His are
involved in metal binding) and contains an active site tyrosine radical. The
regions of the sequence that contain the metal-binding residues and the active
site tyrosine are conserved in ribonucleotide reductase small chain from
prokaryotes, eukaryotes and viruses.
We have selected one of these regions as a signature pattern. It contains the
active site residue as well as a glutamate and a histidine involved in the
binding of iron.
Last update:
December 2001 / Pattern and text revised.
Technical section:
PROSITE method (with tools and information) covered by this documentation:
| RIBORED_SMALL, PS00368; Ribonucleotide reductase small subunit signature (PATTERN) |
| Consensus pattern: |
[IVMSEQ]-E-x(1,2)-[LIVTA]-[HY]-[GSA]-x-[STAVM]-Y-x(2)-[LIVMQ]-x(3)-[LIVFY]-[IVFYCSA]
E and H bind iron, Y is the active site residue |
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE |
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| Matching PDB structures:
1AV8 1H0N 1H0O 1JK0 ... [ALL] |
References:
| 1 |
Authors | Nillson O., Lundqvist T., Hahne S., Sjoberg B.-M. |
| Source | Biochem. Soc. Trans. 16:91-94(1988). |
| 2 |
Authors | Reichard P. |
| Title | From RNA to DNA, why so many ribonucleotide reductases? |
| Source | Science 260:1773-1777(1993). |
| PubMed ID | 8511586 |
| 3 |
Authors | Nordlund P., Sjoberg B.-M., Eklund H. |
| Title | Three-dimensional structure of the free radical protein of ribonucleotide reductase. |
| Source | Nature 345:593-598(1990). |
| PubMed ID | 2190093 |
| DOI | 10.1038/345593a0 |
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