2ALX

Ribonucleotide Reductase R2 from Escherichia coli in space group P6(1)22

Summary for 2ALX

• Entry DOI: 10.2210/pdb2alx/pdb
• Descriptor: Ribonucleoside-diphosphate reductase 1, MANGANESE (II) ION, MERCURY (II) ION (3 entities in total)
• Functional Keywords: ribonucleotide reductase r2, new crystal form, diiron center, dimanganese center, oxidoreductase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 40548.18

Authors

Sommerhalter, M.,Saleh, L.,Bollinger Jr., J.M.,Rosenzweig, A.C. (deposition date: 2005-08-08, release date: 2005-11-29, Last modification date: 2023-08-23)

Primary citation

Sommerhalter, M.,Saleh, L.,Bollinger, J.M.,Rosenzweig, A.C.
Structure of Escherichia coli ribonucleotide reductase R2 in space group P6122.
Acta Crystallogr.,Sect.D, 61:1649-1654, 2005

PubMed Abstract: A new crystal form of wild-type ribonucleotide reductase R2 from Escherichia coli was obtained. Crystals grow in space group P6(1)22 with one R2 monomer in the asymmetric unit. A twofold crystallographic symmetry axis generates the physiological dimeric form of R2. Co-crystallization with CoCl(2) or MnCl(2) results in full occupancy of the dinuclear metal site. The structure of the Mn(II)-loaded form was determined to 2.6 Angstroms resolution by molecular replacement. The crystallization conditions, backbone conformation, crystal-packing interactions and metal centers are compared with those of previously determined crystal forms.

PubMed: 16301799
DOI: 10.1107/S0907444905034062

Experimental method

X-RAY DIFFRACTION (2.6 Å)