1uzr: Difference between revisions

Revision as of 16:30, 21 February 2008

CRYSTAL STRUCTURE OF THE CLASS IB RIBONUCLEOTIDE REDUCTASE R2F-2 SUBUNIT FROM MYCOBACTERIUM TUBERCULOSIS

OverviewOverview

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.

About this StructureAbout this Structure

1UZR is a Single protein structure of sequence from Mycobacterium tuberculosis with , and as ligands. Active as Ribonucleoside-diphosphate reductase, with EC number 1.17.4.1 Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the biologically active form of class Ib ribonucleotide reductase small subunit from Mycobacterium tuberculosis., Uppsten M, Davis J, Rubin H, Uhlin U, FEBS Lett. 2004 Jul 2;569(1-3):117-22. PMID:15225619

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 ==Overview==
-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.
+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.
 ==About this Structure==
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 [[Category: tuberculosis]]
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