Literature DB >> 17008712

The origami of thioredoxin-like folds.

Jonathan L Pan1, James C A Bardwell.   

Abstract

Origami is the Japanese art of folding a piece of paper into complex shapes and forms. Much like origami of paper, Nature has used conserved protein folds to engineer proteins for a particular task. An example of a protein family, which has been used by Nature numerous times, is the thioredoxin superfamily. Proteins in the thioredoxin superfamily are all structured with a beta-sheet core surrounded with alpha-helices, and most contain a canonical CXXC motif. The remarkable feature of these proteins is that the link between them is the fold; however, their reactivity is different for each member due to small variations in this general fold as well as their active site. This review attempts to unravel the minute differences within this protein family, and it also demonstrates the ingenuity of Nature to use a conserved fold to generate a diverse collection of proteins to perform a number of different biochemical tasks.

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Year:  2006        PMID: 17008712      PMCID: PMC2242382          DOI: 10.1110/ps.062268106

Source DB:  PubMed          Journal:  Protein Sci        ISSN: 0961-8368            Impact factor:   6.725


  77 in total

1.  An engineered pathway for the formation of protein disulfide bonds.

Authors:  Lluis Masip; Jonathan L Pan; Suranjana Haldar; James E Penner-Hahn; Matthew P DeLisa; George Georgiou; James C A Bardwell; Jean-François Collet
Journal:  Science       Date:  2004-02-20       Impact factor: 47.728

2.  Glutathione-dependent synthesis of deoxyribonucleotides. Characterization of the enzymatic mechanism of Escherichia coli glutaredoxin.

Authors:  A Holmgren
Journal:  J Biol Chem       Date:  1979-05-10       Impact factor: 5.157

3.  Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione.

Authors:  A Holmgren
Journal:  Proc Natl Acad Sci U S A       Date:  1976-07       Impact factor: 11.205

4.  Glutathione-dependent synthesis of deoxyribonucleotides. Purification and characterization of glutaredoxin from Escherichia coli.

Authors:  A Holmgren
Journal:  J Biol Chem       Date:  1979-05-10       Impact factor: 5.157

5.  Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution.

Authors:  A Holmgren; B O Söderberg; H Eklund; C I Brändén
Journal:  Proc Natl Acad Sci U S A       Date:  1975-06       Impact factor: 11.205

6.  Experimental determination and system level analysis of essential genes in Escherichia coli MG1655.

Authors:  S Y Gerdes; M D Scholle; J W Campbell; G Balázsi; E Ravasz; M D Daugherty; A L Somera; N C Kyrpides; I Anderson; M S Gelfand; A Bhattacharya; V Kapatral; M D'Souza; M V Baev; Y Grechkin; F Mseeh; M Y Fonstein; R Overbeek; A-L Barabási; Z N Oltvai; A L Osterman
Journal:  J Bacteriol       Date:  2003-10       Impact factor: 3.490

7.  Crystal structure of Escherichia coli thiol peroxidase in the oxidized state: insights into intramolecular disulfide formation and substrate binding in atypical 2-Cys peroxiredoxins.

Authors:  Jongkeun Choi; Soonwoong Choi; Jungwon Choi; Mee-Kyung Cha; Il-Han Kim; Whanchul Shin
Journal:  J Biol Chem       Date:  2003-09-23       Impact factor: 5.157

8.  In vivo substrate specificity of periplasmic disulfide oxidoreductases.

Authors:  Annie Hiniker; James C A Bardwell
Journal:  J Biol Chem       Date:  2004-01-15       Impact factor: 5.157

9.  The glutaredoxin -C-P-Y-C- motif: influence of peripheral residues.

Authors:  Nicolas Foloppe; Lennart Nilsson
Journal:  Structure       Date:  2004-02       Impact factor: 5.006

Review 10.  Protein disulfide bond formation in prokaryotes.

Authors:  Hiroshi Kadokura; Federico Katzen; Jon Beckwith
Journal:  Annu Rev Biochem       Date:  2003-01-09       Impact factor: 23.643

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  30 in total

1.  Escherichia coli thioredoxin-like protein YbbN contains an atypical tetratricopeptide repeat motif and is a negative regulator of GroEL.

Authors:  Jiusheng Lin; Mark A Wilson
Journal:  J Biol Chem       Date:  2011-04-15       Impact factor: 5.157

2.  Detecting evolutionary relationships across existing fold space, using sequence order-independent profile-profile alignments.

Authors:  Lei Xie; Philip E Bourne
Journal:  Proc Natl Acad Sci U S A       Date:  2008-04-02       Impact factor: 11.205

Review 3.  Multiple catalytically active thioredoxin folds: a winning strategy for many functions.

Authors:  Emilia Pedone; Danila Limauro; Katia D'Ambrosio; Giuseppina De Simone; Simonetta Bartolucci
Journal:  Cell Mol Life Sci       Date:  2010-07-13       Impact factor: 9.261

4.  New role of the disulfide stress effector YjbH in β-lactam susceptibility of Staphylococcus aureus.

Authors:  Nadine Göhring; Iris Fedtke; Guoqing Xia; Ana M Jorge; Mariana G Pinho; Ute Bertsche; Andreas Peschel
Journal:  Antimicrob Agents Chemother       Date:  2011-09-26       Impact factor: 5.191

Review 5.  Interplay between redox and protein homeostasis.

Authors:  Diogo R Feleciano; Kristin Arnsburg; Janine Kirstein
Journal:  Worm       Date:  2016-03-30

6.  A New Class of Thioredoxin-Related Protein Able to Bind Iron-Sulfur Clusters.

Authors:  Hugo Bisio; Mariana Bonilla; Bruno Manta; Martín Graña; Valentina Salzman; Pablo S Aguilar; Vadim N Gladyshev; Marcelo A Comini; Gustavo Salinas
Journal:  Antioxid Redox Signal       Date:  2015-10-27       Impact factor: 8.401

Review 7.  Bacterial Defense Systems against the Neutrophilic Oxidant Hypochlorous Acid.

Authors:  Sadia Sultana; Alessandro Foti; Jan-Ulrik Dahl
Journal:  Infect Immun       Date:  2020-06-22       Impact factor: 3.441

8.  Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue.

Authors:  Guoping Ren; Daniel Stephan; Zhaohui Xu; Ying Zheng; Danming Tang; Rosemary S Harrison; Mareike Kurz; Russell Jarrott; Stephen R Shouldice; Annie Hiniker; Jennifer L Martin; Begoña Heras; James C A Bardwell
Journal:  J Biol Chem       Date:  2009-01-30       Impact factor: 5.157

9.  Structure and function of Bacillus subtilis YphP, a prokaryotic disulfide isomerase with a CXC catalytic motif .

Authors:  Urszula Derewenda; Tomasz Boczek; Kelly L Gorres; Minmin Yu; Li-wei Hung; David Cooper; Andrzej Joachimiak; Ronald T Raines; Zygmunt S Derewenda
Journal:  Biochemistry       Date:  2009-09-15       Impact factor: 3.162

10.  An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations.

Authors:  Holly J Atkinson; Patricia C Babbitt
Journal:  PLoS Comput Biol       Date:  2009-10-23       Impact factor: 4.475

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