1UZR

Crystal Structure of the Class Ib Ribonucleotide Reductase R2F-2 subunit from Mycobacterium tuberculosis

Summary for 1UZR

• Entry DOI: 10.2210/pdb1uzr/pdb
• Descriptor: RIBONUCLEOTIDE REDUCTASE R2-2 SMALL SUBUNIT, FE (III) ION, CITRIC ACID, ... (5 entities in total)
• Functional Keywords: reductase, ribonucleotide reductase, tuberculosis, r2f-2, radical generation, small subunit
• Biological source: MYCOBACTERIUM TUBERCULOSIS
• Total number of polymer chains: 3
• Total formula weight: 102713.96

Authors

Uppsten, M.,Davis, J.,Rubin, H.,Uhlin, U. (deposition date: 2004-03-15, release date: 2004-07-08, Last modification date: 2023-12-13)

Primary citation

Uppsten, M.,Davis, J.,Rubin, H.,Uhlin, U.
Crystal Structure of the Biologically Active Form of Class Ib Ribonucleotide Reductase Small Subunit from Mycobacterium Tuberculosis
FEBS Lett., 569:117-, 2004

PubMed Abstract: Two nrdF genes of Mycobacterium tuberculosis code for different R2 subunits of the class Ib ribonucleotide reductase (RNR). The proteins are denoted R2F-1 and R2F-2 having 71% sequence identity. The R2F-2 subunit forms the biologically active RNR complex with the catalytic R1E-subunit. We present the structure of the reduced R2F-2 subunit to 2.2 A resolution. Comparison of the R2F-2 structure with a model of R2F-1 suggests that the important differences are located at the C-terminus. We found that within class Ib, the E-helix close to the iron diiron centre has two preferred conformations, which cannot be explained by the redox-state of the diiron centre. In the R2F-2 structure, we also could see a mobility of alphaE in between the two conformations.

PubMed: 15225619
DOI: 10.1016/J.FEBSLET.2004.05.059

Experimental method

X-RAY DIFFRACTION (2.2 Å)