Literature DB >> 11551466

Stability, catalytic versatility and evolution of the (beta alpha)(8)-barrel fold.

B Höcker1, C Jürgens, M Wilmanns, R Sterner.   

Abstract

The (beta alpha)(8)-barrel is a versatile single-domain protein fold that is adopted by a large number of enzymes. The (beta alpha)(8)-barrel fold has been used as a model to elucidate the structural basis of protein thermostability and in studies to interconvert catalytic activities or substrate specificities by rational design or directed evolution. Recently, the (beta alpha)(4)-half-barrel was identified as a possible structural subdomain.

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Year:  2001        PMID： 11551466     DOI： 10.1016/s0958-1669(00)00230-5

Source DB:  PubMed          Journal:  Curr Opin Biotechnol        ISSN： 0958-1669            Impact factor:   9.740


  28 in total

1.  Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry.

Authors:  Olga Mayans; Andreas Ivens; L Johan Nissen; Kasper Kirschner; Matthias Wilmanns
Journal:  EMBO J       Date:  2002-07-01       Impact factor: 11.598

2.  On the structural and functional modularity of glycinamide ribonucleotide formyltransferases.

Authors:  Seung-Goo Lee; Stefan Lutz; Stephen J Benkovic
Journal:  Protein Sci       Date:  2003-10       Impact factor: 6.725

3.  Chimeric cellulase matrix for investigating intramolecular synergism between non-hydrolytic disruptive functions of carbohydrate-binding modules and catalytic hydrolysis.

Authors:  Yuguo Wang; Rentao Tang; Jin Tao; Xiaonan Wang; Baisong Zheng; Yan Feng
Journal:  J Biol Chem       Date:  2012-07-09       Impact factor: 5.157

4.  Two-step Ligand Binding in a (βα)8 Barrel Enzyme: SUBSTRATE-BOUND STRUCTURES SHED NEW LIGHT ON THE CATALYTIC CYCLE OF HisA.

Authors:  Annika Söderholm; Xiaohu Guo; Matilda S Newton; Gary B Evans; Joakim Näsvall; Wayne M Patrick; Maria Selmer
Journal:  J Biol Chem       Date:  2015-08-20       Impact factor: 5.157

5.  Mimicking enzyme evolution by generating new (betaalpha)8-barrels from (betaalpha)4-half-barrels.

Authors:  Birte Höcker; Jörg Claren; Reinhard Sterner
Journal:  Proc Natl Acad Sci U S A       Date:  2004-11-11       Impact factor: 11.205

6.  Characterization of the mutant β-subunit of β-hexosaminidase for dimer formation responsible for the adult form of Sandhoff disease with the motor neuron disease phenotype.

Authors:  Kenichiro Yamada; Yuhei Takado; Yusuke S Kato; Yasukazu Yamada; Hideaki Ishiguro; Nobuaki Wakamatsu
Journal:  J Biochem       Date:  2012-11-05       Impact factor: 3.387

Review 7.  A short history of RubisCO: the rise and fall (?) of Nature's predominant CO2 fixing enzyme.

Authors:  Tobias J Erb; Jan Zarzycki
Journal:  Curr Opin Biotechnol       Date:  2017-08-29       Impact factor: 9.740

8.  Heterogeneity in the structural dynamics of Sulfolobus solfataricus beta-glycosidase revealed by electron paramagnetic resonance and frequency domain fluorometry.

Authors:  Evgenia Lozinsky; Ferdinando Febbraio; Alexander I Shames; Gertz I Likhtenshtein; Ettore Bismuto; Roberto Nucci
Journal:  Protein Sci       Date:  2002-11       Impact factor: 6.725

9.  Reflections on the catalytic power of a TIM-barrel.

Authors:  John P Richard; Xiang Zhai; M Merced Malabanan
Journal:  Bioorg Chem       Date:  2014-07-11       Impact factor: 5.275

10.  Clusters of branched aliphatic side chains serve as cores of stability in the native state of the HisF TIM barrel protein.

Authors:  Basavanapura N Gangadhara; Jennifer M Laine; Sagar V Kathuria; Francesca Massi; C Robert Matthews
Journal:  J Mol Biol       Date:  2013-01-16       Impact factor: 5.469
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