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A novel ADP- and zinc-binding fold from function-directed in vitro evolution.

Paola Lo Surdo1, Martin A Walsh, Maurizio Sollazzo

  • 1Istituto di Ricerche di Biologia Molecolare (IRBM), Via Pontina Km 30.600, 00040 Pomezia, Roma, Italy. paola_losurdo@merck.com

Nature Structural & Molecular Biology
|March 17, 2004
PubMed
Summary

Researchers created a novel protein fold using in vitro evolution. This protein binds adenosine triphosphate (ATP) and is stabilized by a zinc ion, offering a new approach to protein design.

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Area of Science:

  • Protein engineering
  • Structural biology
  • Biochemistry

Background:

  • Designing proteins with novel folds and functions is a significant challenge in biology.
  • De novo protein design is one approach, but alternatives are sought.

Purpose of the Study:

  • To investigate the structure of a randomly generated protein designed to bind adenosine triphosphate (ATP).
  • To explore an alternative strategy to de novo protein design.

Main Methods:

  • In vitro evolution was used to generate a protein library.
  • Randomly generated proteins were screened for ATP binding.
  • Crystal structure determination was performed on the selected protein.

Main Results:

Related Experiment Videos

  • A novel alpha/beta protein fold was discovered.
  • The protein structure was determined in complex with its ligand (ATP).
  • This represents the first protein structure obtained through in vitro evolution.
  • It is also the first nucleotide-binding protein stabilized by a zinc ion.

    • Conclusions:

    • In vitro evolution can yield proteins with novel folds and functions.
    • Zinc-stabilized nucleotide-binding proteins can be generated using this method.
    • This study provides a new structural framework for protein design and engineering.