RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI

Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding.

Structure of Ribonucleotide Reductase Protein R1

DOUBLE FLAT CRYSTAL FIXED-EXIT MONOCHROMATOR USING SI(111) FLATS

PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION

RIBONUCLEOTIDE REDUCTASE R1 PROTEIN, RIBONUCLEOTIDE REDUCTASE R2 PROTEIN, ADENOSINE-5'-TRIPHOSPHATE

RIBONUCLEOTIDE REDUCTASE, DEOXYRIBONUCLEOTIDE SYNTHESIS, RADICAL CHEMISTRY, ALLOSTERIC REGULATION, SPECIFICITY, COMPLEX (OXIDOREDUCTASE-PEPTIDE), COMPLEX (OXIDOREDUCTASE-PEPTIDE) complex

RESIDUES INVOLVED IN BINDING AMPPNP (ATP) AT THE ACTIVITY SITE. THE ACTIVITY SITE REGULATES THE ACTIVITY. EFFECTORS THAT CAN BIND ARE ATP (ACTIVATOR) OR DATP (INHIBITOR).

ACTIVE SITE, THE REDOX CENTER, CYS A 225 AND CYS A 462, IN THE OXIDIZED FORM.

ACTIVE SITE, THE REDOX CENTER, CYS B 225 AND CYS B 462, IN THE OXIDIZED FORM.

ACTIVE SITE, THE REDOX CENTER, CYS C 225 AND CYS C 462, IN THE OXIDIZED FORM.