Literature DB >> 14644177

Evolutionary markers in the (beta/alpha)8-barrel fold.

M Cristina Vega1, Esben Lorentzen, Anni Linden, Matthias Wilmanns.   

Abstract

Enzymes with the (beta/alpha)(8)-barrel fold are involved in the catalysis of a wide variety of biochemical reactions. The active sites of these enzymes are located on the C-terminal face of the central beta-barrel. Conserved amino acid sequence, as well as secondary, tertiary and quaternary structure patterns are providing a rich body of data to support the premise of a common ancestry of many members of the (beta/alpha)(8)-barrel fold family of enzymes. Recent data indicate that there is at least one example of a bienzyme that functions as an ammonia channel, adding a new level of functional diversity to the (beta/alpha)(8)-barrel fold. These proteins have become ideal tools that can be used in conjunction with directed evolution techniques to engineer novel catalytic activities.

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Year:  2003        PMID: 14644177     DOI: 10.1016/j.cbpa.2003.10.004

Source DB:  PubMed          Journal:  Curr Opin Chem Biol        ISSN: 1367-5931            Impact factor:   8.822


  14 in total

1.  Structure of the signal transduction protein TRAP (target of RNAIII-activating protein).

Authors:  Kim Henrick; Miriam Hirshberg
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2012-06-22

2.  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

3.  Two-fold repeated (betaalpha)4 half-barrels may provide a molecular tool for dual substrate specificity.

Authors:  Jochen Kuper; Catharina Doenges; Matthias Wilmanns
Journal:  EMBO Rep       Date:  2005-02       Impact factor: 8.807

4.  Mapping the structure of folding cores in TIM barrel proteins by hydrogen exchange mass spectrometry: the roles of motif and sequence for the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus.

Authors:  Zhenyu Gu; Jill A Zitzewitz; C Robert Matthews
Journal:  J Mol Biol       Date:  2007-02-20       Impact factor: 5.469

Review 5.  The aldo-keto reductase superfamily and its role in drug metabolism and detoxification.

Authors:  Oleg A Barski; Srinivas M Tipparaju; Aruni Bhatnagar
Journal:  Drug Metab Rev       Date:  2008       Impact factor: 4.518

6.  Bisubstrate specificity in histidine/tryptophan biosynthesis isomerase from Mycobacterium tuberculosis by active site metamorphosis.

Authors:  Anne V Due; Jochen Kuper; Arie Geerlof; Jens Peter von Kries; Matthias Wilmanns
Journal:  Proc Natl Acad Sci U S A       Date:  2011-02-14       Impact factor: 11.205

7.  Structure of the methanofuran/methanopterin-biosynthetic enzyme MJ1099 from Methanocaldococcus jannaschii.

Authors:  Thomas A Bobik; Erick J Morales; Annie Shin; Duilio Cascio; Michael R Sawaya; Mark Arbing; Todd O Yeates; Madeline E Rasche
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2014-10-25       Impact factor: 1.056

8.  Modulation of inhibitory activity of xylanase-α-amylase inhibitor protein (XAIP): binding studies and crystal structure determination of XAIP-II from Scadoxus multiflorus at 1.2 Å resolution.

Authors:  Sanjit Kumar; Nagendra Singh; Biswajit Mishra; Divya Dube; Mau Sinha; S Baskar Singh; Sharmistha Dey; Punit Kaur; Sujata Sharma; Tej P Singh
Journal:  BMC Struct Biol       Date:  2010-11-20

9.  A novel chromate reductase from Thermus scotoductus SA-01 related to old yellow enzyme.

Authors:  Diederik Johannes Opperman; Lizelle Ann Piater; Esta van Heerden
Journal:  J Bacteriol       Date:  2008-02-08       Impact factor: 3.490

10.  The UlaG protein family defines novel structural and functional motifs grafted on an ancient RNase fold.

Authors:  Francisco J Fernandez; Fernando Garces; Miguel López-Estepa; Juan Aguilar; Laura Baldomà; Miquel Coll; Josefa Badia; M Cristina Vega
Journal:  BMC Evol Biol       Date:  2011-09-26       Impact factor: 3.260

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