1L1L

CRYSTAL STRUCTURE OF B-12 DEPENDENT (CLASS II) RIBONUCLEOTIDE REDUCTASE

Summary for 1L1L

• Entry DOI: 10.2210/pdb1l1l/pdb
• Descriptor: RIBONUCLEOSIDE TRIPHOSPHATE REDUCTASE (2 entities in total)
• Functional Keywords: 10-stranded alpha-beta barrel, central finger loop, oxidoreductase
• Biological source: Lactobacillus leichmannii
• Total number of polymer chains: 4
• Total formula weight: 328283.88

Authors

Sintchak, M.D.,Arjara, G.,Kellogg, B.A.,Stubbe, J.,Drennan, C.L. (deposition date: 2002-02-18, release date: 2002-04-10, Last modification date: 2024-10-16)

Primary citation

Sintchak, M.D.,Arjara, G.,Kellogg, B.A.,Stubbe, J.,Drennan, C.L.
The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer.
Nat.Struct.Biol., 9:293-300, 2002

PubMed Abstract: Ribonucleotide reductases (RNRs) catalyze the conversion of ribonucleotides to deoxyribonucleotides, an essential step in DNA biosynthesis and repair. Here we present the crystal structure of class II (coenzyme B12-dependent) ribonucleoside triphosphate reductase (RTPR) from Lactobacillus leichmannii in the apo enzyme form and in complex with the B12 analog adeninylpentylcobalamin at 1.75 and 2.0 A resolution, respectively. This monomeric, allosterically regulated class II RNR retains all the key structural features associated with the catalytic and regulatory machinery of oligomeric RNRs. Surprisingly, the dimer interface responsible for effector binding in class I RNR is preserved through a single 130-residue insertion in the class II structure. Thus, L. leichmannii RNR is a paradigm for the simplest structural entity capable of ribonucleotide reduction, a reaction linking the RNA and DNA worlds.

PubMed: 11875520
DOI: 10.1038/nsb774

Experimental method

X-RAY DIFFRACTION (1.75 Å)