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Structure of the hypothetical Mycoplasma protein MPN555 suggests a chaperone function

Ursula Schulze-Gahmen1, Shelly Aono, Shengfeng Chen

  • 1Berkeley Structural Genomics Center, Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.

Acta Crystallographica. Section D, Biological Crystallography
|October 6, 2005
PubMed

Insights

The crystal structure of Mycoplasma pneumoniae hypothetical protein MPN555 was determined, revealing a three-lobed, alpha-helical fold. This structure suggests MPN555 functions as a molecular chaperone involved in protein folding.

Area of Science:

  • Structural biology
  • Mycoplasma pneumoniae research
  • Protein structure determination

Background:

  • Hypothetical proteins represent a significant portion of the proteome in many organisms, including Mycoplasma pneumoniae.
  • Understanding the structure and function of these proteins is crucial for elucidating cellular mechanisms.

Purpose of the Study:

  • To determine the three-dimensional crystal structure of the hypothetical protein MPN555 from Mycoplasma pneumoniae.
  • To investigate the potential function of MPN555 based on its structural characteristics and homology.

Main Methods:

  • X-ray crystallography was employed to determine the crystal structure.
  • Anomalous diffraction data at the Selenium (Se) peak wavelength was utilized.
  • Structure resolution was achieved to 2.8 Angstrom.

Main Results:

  • The crystal structure of MPN555 revealed a predominantly alpha-helical protein with a distinct three-lobed or 'three-finger' shape.
  • The protein possesses a central binding groove and additional grooves between lobes.
  • A peptide from an N-terminal affinity tag occupied the central binding pocket in one molecule.
  • MPN555 exhibits structural homology to bacterial chaperone proteins SurA and trigger factor.

Conclusions:

  • The determined structure of MPN555 provides insights into its molecular architecture.
  • Structural homology to known chaperone proteins suggests a role for MPN555 in protein folding as a molecular chaperone.

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