Structure of the Hypothetical Protein PF0899 from Pyrococcus furiosus at 1.85 A Resolution

Laura-Lee Clancy Kelley, Bret D. Dillard, Wolfram Tempel, Lirong Chen, Neil Shaw, Doowon Lee, M. Gary Newton, Frank J. Sugar, Francis E. Jenney, Han Seung Lee, Claudia Shah, Farris L. Poole, Michael W. W. Adams, Jane S. Richardson, David C. Richardson, Zhi-Jie Liu, Bi-Cheng Wang, John Rose

Research output: Contribution to journalArticlepeer-review

Abstract

The hypothetical protein PF0899 is a 95-residue peptide from the hyperthermophilic archaeon Pyrococcus furiosus that represents a gene family with six members. P. furiosus ORF PF0899 has been cloned, expressed and crystallized and its structure has been determined by the Southeast Collaboratory for Structural Genomics (http://www.secsg.org). The structure was solved using the SCA2Structure pipeline from multiple data sets and has been refined to 1.85 A against the highest resolution data set collected (a presumed gold derivative), with a crystallographic R factor of 21.0% and R(free) of 24.0%. The refined structure shows some structural similarity to a wedge-shaped domain observed in the structure of the major capsid protein from bacteriophage HK97, suggesting that PF0899 may be a structural protein.

Original languageAmerican English
JournalActa Crystallographica Section F, Structural Biology and Crystallization Communications
Volume63
StatePublished - Jul 1 2007

Keywords

  • Archaeal Proteins
  • Cloning
  • Molecular
  • Crystallization
  • Crystallography
  • X-Ray
  • Open Reading Frames
  • Protein Structure
  • Secondary
  • Pyrococcus furiosus

Disciplines

  • Genomics
  • Medicine and Health Sciences
  • Structural Biology

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