Sandbox 46
From Proteopedia
| Line 6: | Line 6: | ||
1w68 (under oxidizing conditions) | 1w68 (under oxidizing conditions) | ||
| - | 1w69 (under reducing conditions) | + | 1w69 (under reducing conditions)<ref>http://blast.ncbi.nlm.nih.gov/Blast.cgi</ref> |
==Introduction== | ==Introduction== | ||
| - | Mouse ribonucleotide reductase is a class I enzyme. Class I enzymes consist of two different subunits. These two subunits are connected via hydrogen bonds. This enzyme acts primarily to catalyze the reduction of nucleoside diphosphates to deoxynucleoside diphosphates. Within DNA synthesis, this is the first dedicated step. The R2 subunit, a homodimer, is the smaller of the two subunits in this enzyme and serves as a limiting agent for overall enzyme activity. This subunit acts to maintain the tyrosil radical neighboring a diiron carboxylate site. In the mouse R2 subunit, the tyrosine residue is Tyr177. Through the process of catalysis, it has been proposed that the oxidation equivalent stored in the tyrosil subunit is passed along a pathway to a cysteine residue at an active site. Both subunits act as electron transfer pathways to the iron site. An arginine residue, Arg 265, has proven to be key to the activity of this particular enzyme. | + | Mouse ribonucleotide reductase is a class I enzyme. Class I enzymes consist of two different subunits. These two subunits are connected via hydrogen bonds. This enzyme acts primarily to catalyze the reduction of nucleoside diphosphates to deoxynucleoside diphosphates. Within DNA synthesis, this is the first dedicated step. The R2 subunit, a homodimer, is the smaller of the two subunits in this enzyme and serves as a limiting agent for overall enzyme activity. This subunit acts to maintain the tyrosil radical neighboring a diiron carboxylate site. In the mouse R2 subunit, the tyrosine residue is Tyr177. Through the process of catalysis, it has been proposed that the oxidation equivalent stored in the tyrosil subunit is passed along a pathway to a cysteine residue at an active site. Both subunits act as electron transfer pathways to the iron site. An arginine residue, Arg 265, has proven to be key to the activity of this particular enzyme. <ref>http://www.jbc.org/cgi/content/full/281/36/26022</ref> |
==Structual Properties== | ==Structual Properties== | ||
While both forms of this enzyme both interact with iron, there are some structural differences due to the different conditions. | While both forms of this enzyme both interact with iron, there are some structural differences due to the different conditions. | ||
| Line 19: | Line 19: | ||
1w69: | 1w69: | ||
15 α-helices | 15 α-helices | ||
| - | 10 β-turns | + | 10 β-turns<ref>http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/</ref> |
==Protein Sequence== | ==Protein Sequence== | ||
| Line 36: | Line 36: | ||
KKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFA | KKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFA | ||
CLMFKHLVHKPAEQRVREIITNAVRIEQEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFNKIFR | CLMFKHLVHKPAEQRVREIITNAVRIEQEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFNKIFR | ||
| - | VENPF | + | VENPF<ref>http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/</ref> |
Revision as of 20:40, 10 October 2008
Template:STRUCTURE 1w68 Template:STRUCTURE 1w69
Contents |
Mouse Ribonucleotide Reductase R2
Protein ID:
1w68 (under oxidizing conditions)
1w69 (under reducing conditions)[1]
Introduction
Mouse ribonucleotide reductase is a class I enzyme. Class I enzymes consist of two different subunits. These two subunits are connected via hydrogen bonds. This enzyme acts primarily to catalyze the reduction of nucleoside diphosphates to deoxynucleoside diphosphates. Within DNA synthesis, this is the first dedicated step. The R2 subunit, a homodimer, is the smaller of the two subunits in this enzyme and serves as a limiting agent for overall enzyme activity. This subunit acts to maintain the tyrosil radical neighboring a diiron carboxylate site. In the mouse R2 subunit, the tyrosine residue is Tyr177. Through the process of catalysis, it has been proposed that the oxidation equivalent stored in the tyrosil subunit is passed along a pathway to a cysteine residue at an active site. Both subunits act as electron transfer pathways to the iron site. An arginine residue, Arg 265, has proven to be key to the activity of this particular enzyme. [2]
Structual Properties
While both forms of this enzyme both interact with iron, there are some structural differences due to the different conditions.
1w68: 16 α-helices 8 β-turns
1w69: 15 α-helices 10 β-turns[3]
Protein Sequence
For the enzyme under oxidizing conditions (1w68):
VEDEPLLRENPRRFVVFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWEALKPDERHFISHVLAFFA ASDGIVNENLVERFSQEVQVTEARCFYGFQIAMENIHSEMYSLLIDTYIKDPKEREYLFNAIETMPCVK KKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFA CLMFKHLVHKPAEQRVREIITNAVRIEQEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFNKIFR VENPF
For the enzyme under reducing conditions(1w69):
VEDEPLLRENPRRFVVFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWEALKPDERHFISHVLAFFA ASDGIVNENLVERFSQEVQVTEARCFYGFQIAMENIHSEMYSLLIDTYIKDPKEREYLFNAIETMPCVK KKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFA CLMFKHLVHKPAEQRVREIITNAVRIEQEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFNKIFR VENPF[4]
