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Structural biology.

K C Holmes1

  • 1Max-Planck-Institut für medizinische Forschung, Heidelberg, Germany. holmes@mpimf-heidelberg.mpg.de

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
|February 12, 2000
PubMed
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Protein crystallography, aided by synchrotron radiation and gene expression in Escherichia coli, reveals universal protein folds. This structural data aids function prediction and future biochemical research.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Genomics

Background:

  • Protein crystallography is crucial for understanding cellular mechanisms.
  • Advances in data collection, synchrotron radiation, and gene expression have propelled the field.
  • All proteins are constructed from approximately 1000 fundamental folds, with about 450 currently identified.

Purpose of the Study:

  • To explore the predictive power of protein structure from sequence data.
  • To investigate the potential of determining structures from bacterial genomes to infer protein function.
  • To anticipate future demands and challenges in structural biology.

Main Methods:

  • Analysis of known protein structures to identify common folds.
  • Utilizing synchrotron radiation for advanced data collection in protein crystallography.

Related Experiment Videos

  • Employing gene expression in Escherichia coli for protein structure determination.

    • Main Results:

    • Identification of around 1000 primordial protein folds, forming the basis for structure prediction.
    • A limited fraction of sequenced genomes can be functionally annotated based on sequence homology alone.
    • Structural determination from bacterial genomes is an ongoing effort to link structure to function.

    Conclusions:

    • The collection of primeval folds is essential for predicting protein structure from sequence.
    • Determining protein structures is more reliable for function prediction than sequence analysis alone.
    • The field anticipates a significant increase in protein structure determination, requiring enhanced synchrotron capabilities and more biochemists.