scholarly journals Structural Basis for Superoxide Activation of Flavobacterium johnsoniae Class I Ribonucleotide Reductase and for Radical Initiation by Its Dimanganese Cofactor

Biochemistry ◽  
2018 ◽  
Vol 57 (18) ◽  
pp. 2679-2693 ◽  
Author(s):  
Hannah R. Rose ◽  
Manas K. Ghosh ◽  
Ailiena O. Maggiolo ◽  
Christopher J. Pollock ◽  
Elizabeth J. Blaesi ◽  
...  
Keyword(s):  
Ribonucleotide Reductase ◽  
Class I ◽  
Structural Basis ◽  
Radical Initiation ◽  
Flavobacterium Johnsoniae

Radical Initiation in the Class I Ribonucleotide Reductase: Long-Range Proton-Coupled Electron Transfer?

ChemInform ◽  
2003 ◽  
Vol 34 (32) ◽  
Author(s):  
JoAnne Stubbe ◽  
Daniel G. Nocera ◽  
Cyril S. Yee ◽  
Michelle C. Y. Chang
Keyword(s):  
Electron Transfer ◽  
Long Range ◽  
Ribonucleotide Reductase ◽  
Class I ◽  
Radical Initiation ◽  
Proton Coupled Electron Transfer

scholarly journals Solution Structure of the dATP-Inactivated Class I Ribonucleotide Reductase From Leeuwenhoekiella blandensis by SAXS and Cryo-Electron Microscopy

2021 ◽  
Vol 8 ◽  
Author(s):  
Mahmudul Hasan ◽  
Ipsita Banerjee ◽  
Inna Rozman Grinberg ◽  
Britt-Marie Sjöberg ◽  
Derek T. Logan
Keyword(s):  
Ribonucleotide Reductase ◽  
Solution Structure ◽  
Three Dimensional ◽  
Class I ◽  
Structural Basis ◽  
Α Subunit ◽  
Cryo Electron Microscopy ◽  
N Terminus ◽  
Small Domain ◽  
Essential Enzyme

The essential enzyme ribonucleotide reductase (RNR) is highly regulated both at the level of overall activity and substrate specificity. Studies of class I, aerobic RNRs have shown that overall activity is downregulated by the binding of dATP to a small domain known as the ATP-cone often found at the N-terminus of RNR subunits, causing oligomerization that prevents formation of a necessary α2β2 complex between the catalytic (α2) and radical generating (β2) subunits. In some relatively rare organisms with RNRs of the subclass NrdAi, the ATP-cone is found at the N-terminus of the β subunit rather than more commonly the α subunit. Binding of dATP to the ATP-cone in β results in formation of an unusual β4 tetramer. However, the structural basis for how the formation of the active complex is hindered by such oligomerization has not been studied. Here we analyse the low-resolution three-dimensional structures of the separate subunits of an RNR from subclass NrdAi, as well as the α4β4 octamer that forms in the presence of dATP. The results reveal a type of oligomer not previously seen for any class of RNR and suggest a mechanism for how binding of dATP to the ATP-cone switches off catalysis by sterically preventing formation of the asymmetrical α2β2 complex.

Radical Initiation in the Class I Ribonucleotide Reductase:  Long-Range Proton-Coupled Electron Transfer?

2003 ◽  
Vol 103 (6) ◽  
pp. 2167-2202 ◽  
Author(s):  
JoAnne Stubbe ◽  
Daniel G. Nocera ◽  
Cyril S. Yee ◽  
Michelle C. Y. Chang
Keyword(s):  
Electron Transfer ◽  
Long Range ◽  
Ribonucleotide Reductase ◽  
Class I ◽  
Radical Initiation ◽  
Proton Coupled Electron Transfer

Peroxo-Type Intermediates in Class I Ribonucleotide Reductase and Related Binuclear Non-Heme Iron Enzymes

2009 ◽  
Vol 131 (34) ◽  
pp. 12155-12171 ◽  
Author(s):  
Kasper P. Jensen ◽  
Caleb B. Bell, ◽  
Michael D. Clay ◽  
Edward I. Solomon
Keyword(s):  
Ribonucleotide Reductase ◽  
Heme Iron ◽  
Class I ◽  
Non Heme Iron ◽  
Iron Enzymes

scholarly journals Selenocysteine Substitution in a Class I Ribonucleotide Reductase

Biochemistry ◽  
2019 ◽  
Vol 58 (50) ◽  
pp. 5074-5084 ◽  
Author(s):  
Brandon L. Greene ◽  
JoAnne Stubbe ◽  
Daniel G. Nocera
Keyword(s):  
Ribonucleotide Reductase ◽  
Class I

scholarly journals Characterization of a Basidiomycota hydrophobin reveals the structural basis for a high-similarity Class I subdivision

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Julie-Anne Gandier ◽  
David N. Langelaan ◽  
Amy Won ◽  
Kylie O’Donnell ◽  
Julie L. Grondin ◽  
...  
Keyword(s):  
Class I ◽  
Structural Basis ◽  
High Similarity ◽  
Similarity Class

scholarly journals Direct Measurement of the Radical Translocation Distance in the Class I Ribonucleotide Reductase fromChlamydia trachomatis

2015 ◽  
Vol 119 (43) ◽  
pp. 13777-13784 ◽  
Author(s):  
Jovan Livada ◽  
Ryan J. Martinie ◽  
Laura M. K. Dassama ◽  
Carsten Krebs ◽  
J. Martin Bollinger ◽  
...  
Keyword(s):  
Direct Measurement ◽  
Ribonucleotide Reductase ◽  
Class I

scholarly journals Genetic and Functional Diversity of Human Immunodeficiency Virus Type 1 Subtype B Nef Primary Isolates

2001 ◽  
Vol 75 (4) ◽  
pp. 1672-1680 ◽  
Author(s):  
John L. Foster ◽  
Rene P. Molina ◽  
Tianci Luo ◽  
Vivek K. Arora ◽  
Yaoxing Huang ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Mhc Class I ◽  
Mutational Analysis ◽  
Infected Individual ◽  
Class I ◽  
Structural Basis ◽  
Amino Acid Residues ◽  
Subtype B ◽  
Immunodeficiency Virus ◽  
Hiv Subtypes

ABSTRACT We have characterized the functional integrity of seven primary Nef isolates: five from a long-term nonprogressing human immunodeficiency virus (HIV)-infected individual and one each from two patients with AIDS. One of the seven Nefs was defective for CD4 downregulation, two others were defective for PAK-2 activation, and one Nef was defective for PAK-2 activation and major histocompatibility complex (MHC) class I downregulation. Five of the Nefs were tested and found to be functional for the enhancement of virus particle infectivity. The structural basis for each of the functional defects has been analyzed by constructing a consensus nef, followed by mutational analysis of the variant amino acid residues. Mutations A29V and F193I were deleterious to CD4 downregulation and PAK-2 activation, respectively, while S189R rendered Nef defective for both MHC class I downregulation and PAK-2 activation. A search of the literature identified HIVs from five patients with Nefs predominantly mutated at F193 and from one patient with Nefs predominantly mutated at A29. A29 is highly conserved in all HIV subtypes except for subtype E. F193 is conserved in subtype B (and possibly in the closely related subtype D), but none of the other HIV group M subtypes. Our results suggest that functional distinctions may exist between HIV subtypes.

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