1PEM

Ribonucleotide Reductase Protein R1E from Salmonella typhimurium

Summary for 1PEM

• Entry DOI: 10.2210/pdb1pem/pdb
• Related: 1PEO 1PEQ 1PEU 1R1R 2R1R
• Descriptor: Ribonucleoside-diphosphate reductase 2 alpha chain (1 entity in total)
• Functional Keywords: 10 stranded alpha/beta barrel, protein-specificity-effector complex, datp, oxidoreductase
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 1
• Total formula weight: 80686.21

Authors

Uppsten, M.,Farnegardh, M.,Jordan, A.,Eliasson, R.,Eklund, H.,Uhlin, U. (deposition date: 2003-05-22, release date: 2004-05-25, Last modification date: 2024-04-03)

Primary citation

Uppsten, M.,Farnegardh, M.,Jordan, A.,Eliasson, R.,Eklund, H.,Uhlin, U.
Structure of the large subunit of class Ib ribonucleotide reductase from Salmonella typhimurium and its complexes with allosteric effectors.
J.Mol.Biol., 330:87-97, 2003

PubMed Abstract: The three-dimensional structure of the large subunit of the first member of a class Ib ribonucleotide reductase, R1E of Salmonella typhimurium, has been determined in its native form and together with three allosteric effectors. The enzyme contains the characteristic ten-stranded alpha/beta-barrel with catalytic residues at a finger loop in its center and with redox-active cysteine residues at two adjacent barrel strands. Structures where the redox-active cysteine residues are in reduced thiol form and in oxidized disulfide form have been determined revealing local structural changes. The R1E enzyme differs from the class Ia enzyme, Escherichia coli R1, by not having an overall allosteric regulation. This is explained from the structure by differences in the N-terminal domain, which is about 50 residues shorter and lacks the overall allosteric binding site. R1E has an allosteric substrate specificity regulation site and the binding site for the nucleotide effectors is located at the dimer interface similarly as for the class Ia enzymes. We have determined the structures of R1E in the absence of effectors and with dTTP, dATP and dCTP bound. The low affinity for ATP at the specificity site is explained by a tyrosine, which hinders nucleotides containing a 2'-OH group to bind.

PubMed: 12818204
DOI: 10.1016/S0022-2836(03)00538-2

Experimental method

X-RAY DIFFRACTION (2.99 Å)