| General information | | DisProt: | DP00462 | | Name: | Ribonucleoside-diphosphate reductase M2 subunit | | Synonym(s): | RIR2_MOUSE
EC=1.17.4.1
Ribonucleotide reductase small subunit
Ribonucleotide reductase small chain
| | First appeared in release: | Release 3.1 (03/31/2006) | | UniProt: | P11157 | | UniGene: | Mm.99 | | SwissProt: | RIR2_MOUSE | | TrEMBL: | | | NCBI (GI): | 132626 | | Source organism: | Mus musculus (Mouse) | | Sequence length: | 390 | | Percent disordered: | 26% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MLSVRTPLAT IADQQQLQLS PLKRLTLADK ENTPPTLSST RVLASKAARR IFQDSAELES - 60
KAPTNPSVED EPLLRENPRR FVVFPIEYHD IWQMYKKAEA SFWTAEEVDL SKDIQHWEAL - 120
KPDERHFISH VLAFFAASDG IVNENLVERF SQEVQVTEAR CFYGFQIAME NIHSEMYSLL - 180
IDTYIKDPKE REYLFNAIET MPCVKKKADW ALRWIGDKEA TYGERVVAFA AVEGIFFSGS - 240
FASIFWLKKR GLMPGLTFSN ELISRDEGLH CDFACLMFKH LVHKPAEQRV REIITNAVRI - 300
EQEFLTEALP VKLIGMNCTL MKQYIEFVAD RLMLELGFNK IFRVENPFDF MENISLEGKT - 360
NFFEKRVGEY QRMGVMSNST ENSFTLDADF
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| Functional narrative |
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 1 - 64 | | Length: | 64 | | Region sequence: |
MLSVRTPLATIADQQQLQLSPLKRLTLADKENTPPTLSSTRVLASKAARRIFQDSAELES
KAPT | | Modification type: | Complex
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (293 K; acetate buffer (pH 4.7) 50 mM; NaCl (0.8-1.0 M))
| References:
- Kauppi B, Nielsen BB, Ramaswamy S, Larsen IK, Thelander M, Thelander L, Eklund H. "The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2." J Mol Biol. 1996; 262(5): 706-20. PubMed: 8876648
- Nielsen BB, Kauppi B, Thelander M, Thelander L, Larsen IK, Eklund H. "Crystallization and crystallographic investigations of the small subunit of mouse ribonucleotide reductase." FEBS Lett. 1995; 373(3): 310-2. PubMed: 7589490
| Comments:The N-terminal residues are not essential for enzymatic activity but the N-terminal tail may function in cell-cycle regulation of the enzyme and protein degradation.
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| Region 2 | | Type: | Disordered | | Name: | | | Location: | 354 - 390 | | Length: | 37 | | Region sequence: |
ISLEGKTNFFEKRVGEYQRMGVMSNSTENSFTLDADF | | Modification type: | Complex
Engineered
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- X-ray crystallography (293 K; acetate buffer (pH 4.7) 50 mM; NaCl (0.8-1.0 M))
- Nuclear magnetic resonance (NMR) (288 K; pH: 6.8; D2O (99.8%); KCl 150 mM; potassium phosphate 10 mM)
| References:
- Kauppi B, Nielsen BB, Ramaswamy S, Larsen IK, Thelander M, Thelander L, Eklund H. "The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2." J Mol Biol. 1996; 262(5): 706-20. PubMed: 8876648
- Lycksell PO, Ingemarson R, Davis R, Graslund A, Thelander L. "1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal tail, essential for subunit interaction, is highly flexible but becomes rigid in the presence of protein R1." Biochemistry. 1994; 33(10): 2838-42. PubMed: 8130196
- Nielsen BB, Kauppi B, Thelander M, Thelander L, Larsen IK, Eklund H. "Crystallization and crystallographic investigations of the small subunit of mouse ribonucleotide reductase." FEBS Lett. 1995; 373(3): 310-2. PubMed: 7589490
| Comments:The C-terminus of R2 is involved in the interaction between R1 and R2. The C-terminal seven residues go from disorder to order upon binding to R1.
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| Comments |
Mouse Ribonucleotide Reductase is made up of two non-identical subunits, R1 and R2, which are both inactive when unbound to each other.
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