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Structure of Vibrio cholerae ribosome hibernation promoting factor.

ABSTRACT: The X-ray crystal structure of ribosome hibernation promoting factor (HPF) from Vibrio cholerae is presented at 2.0?Å resolution. The crystal was phased by two-wavelength MAD using cocrystallized cobalt. The asymmetric unit contained two molecules of HPF linked by four Co atoms. The metal-binding sites observed in the crystal are probably not related to biological function. The structure of HPF has a typical ?-?-?-?-?-? fold consistent with previous structures of YfiA and HPF from Escherichia coli. Comparison of the new structure with that of HPF from E. coli bound to the Thermus thermophilus ribosome [Polikanov et al. (2012), Science, 336, 915-918] shows that no significant structural changes are induced in HPF by binding.

SUBMITTER: De Bari H 

PROVIDER: S-EPMC3606564 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature

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Structure of Vibrio cholerae ribosome hibernation promoting factor.

De Bari Heather H   Berry Edward A EA  

Acta crystallographica. Section F, Structural biology and crystallization communications 20130222 Pt 3

The X-ray crystal structure of ribosome hibernation promoting factor (HPF) from Vibrio cholerae is presented at 2.0 Å resolution. The crystal was phased by two-wavelength MAD using cocrystallized cobalt. The asymmetric unit contained two molecules of HPF linked by four Co atoms. The metal-binding sites observed in the crystal are probably not related to biological function. The structure of HPF has a typical β-α-β-β-β-α fold consistent with previous structures of YfiA and HPF from Escherichia co  ...[more]

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