Cloning, Expression, Crystallization and Preliminary Crystallographic Analysis of a Pentapeptide-repeat Protein (Rfr23) from the Bacterium Cyanothece 51142l
Journal Article
·
· Acta Crystallographica Section F: Structural Biology and Crystallization Communications
A unique feature of cyanobacteria genomes is the abundance of genes that code for hypothetical proteins containing tandem pentapeptide repeats approximately described by the consensus motif A(N/D)LXX. To date, the structures of two pentapeptide-repeat proteins (PRPs) have been determined, with the tandem pentapeptide-repeat sequences observed to adopt a novel type of right-handed quadrilateral {beta}-helix, or Rfr-fold, in both structures. One structure, Mycobacterium tuberculosis MfpA, is a 183-residue protein that contains 30 consecutive pentapeptide repeats and appears to offer antibiotic resistance by acting as a DNA mimic. The other structure, Cyanothece 51142 Rfr32, is a 167-residue protein that contains 21 consecutive pentapeptide repeats. The function of Rfr32, like the other 35 hypothetical PRPs identified in the genome of Cyanothece, is unknown. In an effort to understand the role of PRPs in cyanobacteria and to better characterize the structural properties of Rfr-folds with different amino-acid sequences, a second PRP from Cyanothece 51142, Rfr23, has been cloned, expressed and purified. Selenomethione-substituted protein was crystallized by vapor diffusion in hanging drops. Nearly complete SAD and native diffraction data sets were collected from these crystals to 2.5 and 2.1 {angstrom} resolution, respectively, using synchrotron radiation. The crystals belonged to space group I4{sub 1}, with unit-cell parameters a = b = 106.61, c = 53.37 {angstrom}, and one molecule per asymmetric unit. Preliminary analysis of the electron-density map from the SAD data shows that Rfr23 contains an Rfr-fold.
- Research Organization:
- Brookhaven National Laboratory (BNL) National Synchrotron Light Source
- Sponsoring Organization:
- Doe - Office Of Science
- DOE Contract Number:
- AC02-98CH10886
- OSTI ID:
- 929826
- Report Number(s):
- BNL--80383-2008-JA
- Journal Information:
- Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Journal Name: Acta Crystallographica Section F: Structural Biology and Crystallization Communications Vol. F62
- Country of Publication:
- United States
- Language:
- English
Similar Records
Cloning, expression, crystallization and preliminary crystallographic analysis of a pentapeptide-repeat protein (Rfr23) from bacterium Cyanothece 511421
Pentapeptide Repeat Proteins and Cyanobacteria
Insights into the structural variation between pentapeptide repeat proteins - Crystal structure of Rfr23 from Cyanothece 51142
Journal Article
·
Thu Nov 30 23:00:00 EST 2006
· Acta Crystallographica. Section F, 62(12):1251-1254
·
OSTI ID:897382
Pentapeptide Repeat Proteins and Cyanobacteria
Book
·
Fri Oct 16 00:00:00 EDT 2009
·
OSTI ID:970368
Insights into the structural variation between pentapeptide repeat proteins - Crystal structure of Rfr23 from Cyanothece 51142
Journal Article
·
Thu Apr 10 00:00:00 EDT 2008
· Journal of Structural Biology, 162(1):184-192
·
OSTI ID:927701