Structural insights on two hypothetical secretion chaperones from Xanthomonas axonopodis pv. citri

Protein J. 2011 Jun;30(5):324-33. doi: 10.1007/s10930-011-9335-z.

Abstract

Several Gram-negative bacterial pathogens have developed type III secretion systems (T3SSs) to deliver virulence proteins directly into eukaryotic cells in a process essential for many diseases. The type III secretion processes require customized chaperones with high specificity for binding partners, thus providing the secretion to occur. Due to the very low sequence similarities among secretion chaperones, annotation and discrimination of a great majority of them is extremely difficult and a task with low scores even if genes are encountered that codify for small (<20 kDa) proteins with low pI and a tendency to dimerise. Concerning about this, herein, we present structural features on two hypothetical T3SSs chaperones belonging to plant pathogen Xanthomonas axonopodis pv. citri and suggest how low resolution models based on Small Angle X-ray Scattering patterns can provide new structural insights that could be very helpful in their analysis and posterior classification.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Bacterial Secretion Systems
  • Circular Dichroism
  • Escherichia coli
  • Models, Molecular
  • Molecular Chaperones / chemistry*
  • Molecular Chaperones / metabolism
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Scattering, Small Angle
  • X-Ray Diffraction
  • Xanthomonas axonopodis / chemistry*
  • Xanthomonas axonopodis / metabolism

Substances

  • Bacterial Proteins
  • Bacterial Secretion Systems
  • Molecular Chaperones
  • Recombinant Proteins