Literature DB >> 20153164

Nonribosomal peptide synthetases: structures and dynamics.

Matthias Strieker1, Alan Tanović, Mohamed A Marahiel.   

Abstract

Nonribosomal peptide synthetases (NRPSs) are large multimodular biocatalysts that utilize complex regiospecific and stereospecific reactions to assemble structurally and functionally diverse peptides that have important medicinal applications. During this ribosome-independent peptide synthesis, catalytic domains of NRPS select, activate or modify the covalently tethered reaction intermediates to control the iterative chain elongation process and product release. Recent advances in structural elucidation of domains, didomains, and an entire termination module revealed valuable insights into the mechanism of nonribosomal synthesis and are highlighted herein.

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Year:  2010        PMID: 20153164     DOI: 10.1016/j.sbi.2010.01.009

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  128 in total

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8.  Structure determination of the functional domain interaction of a chimeric nonribosomal peptide synthetase from a challenging crystal with noncrystallographic translational symmetry.

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9.  Predicting substrate specificity of adenylation domains of nonribosomal peptide synthetases and other protein properties by latent semantic indexing.

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