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Structure-based multiple alignment of extracellular pectate lyase sequences

S Heffron1, B Henrissat, M D Yoder

  • 1Department of Biochemistry, University of California, Riverside 92521, USA.

Molecular Plant-Microbe Interactions : MPMI
|March 1, 1995
PubMed
Summary
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Pectate lyases are plant cell wall degrading enzymes. Structural analysis refined their evolutionary alignment, revealing key amino acids for enzymatic function.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Plant Pathology

Background:

  • Pectate lyases are crucial secreted virulence factors.
  • They degrade the pectate component of plant cell walls, facilitating pathogen invasion.
  • Understanding their structure-function relationship is vital for controlling plant diseases.

Purpose of the Study:

  • To refine the evolutionary-based multiple alignment of extracellular pectate lyases.
  • To identify invariant amino acids critical for enzymatic activity using structural data.
  • To elucidate the molecular mechanisms underlying pectate lyase function.

Main Methods:

  • Evolutionary-based multiple sequence alignment of extracellular pectate lyases.
  • Incorporation of three-dimensional structural information from Erwinia chrysanthemi pectate lyases C and E.

Related Experiment Videos

  • Analysis of invariant amino acids within the refined alignment.

    • Main Results:

    • A corrected multiple alignment of extracellular pectate lyases was generated.
    • Invariant amino acids were identified and localized.
    • These invariant residues are strongly implicated in two distinct enzymatic functions.

    Conclusions:

    • The refined alignment provides a more accurate representation of pectate lyase evolution.
    • Specific invariant amino acids are critical for the catalytic activity of these enzymes.
    • This finding advances our understanding of pectate lyase mechanisms and potential targets for disease control.