1l1l
From Proteopedia
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| , resolution 1.75Å | |||||||
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| Activity: | Ribonucleoside-triphosphate reductase, with EC number 1.17.4.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF B-12 DEPENDENT (CLASS II) RIBONUCLEOTIDE REDUCTASE
Overview
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.
About this Structure
1L1L is a Single protein structure of sequence from Lactobacillus leichmannii. Full crystallographic information is available from OCA.
Reference
The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer., Sintchak MD, Arjara G, Kellogg BA, Stubbe J, Drennan CL, Nat Struct Biol. 2002 Apr;9(4):293-300. PMID:11875520
Page seeded by OCA on Sun Mar 30 21:56:42 2008
