1. The molecular structure of Rv1873, a conserved hypothetical protein from Mycobacterium tuberculosis, at 1.38 A resolution.
- Author
-
Garen CR, Cherney MM, Bergmann EM, and James MN
- Subjects
- Amino Acid Sequence, Catalytic Domain, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Sequence Alignment, Bacterial Proteins chemistry, Mycobacterium tuberculosis chemistry, Protein Structure, Tertiary
- Abstract
The X-ray crystal structure of the gene product encoded by open reading frame Rv1873 of Mycobacterium tuberculosis has been determined by single isomorphous replacement with anomalous scattering (SIRAS) phasing techniques at 1.38 A resolution from monoclinic crystals with unit-cell parameters a = 33.44, b = 31.63, c = 53.19 A, beta = 90.8 degrees. The 16.2 kDa Rv1873 is a monomer that adopts a primarily alpha-helical fold with limited structural similarity to previously determined tertiary structures. It has been annotated as a conserved hypothetical protein of unknown function and is classified by the Clusters of Orthologous Groups (COG) database as belonging to COG5579. The three-dimensional structure of the Rv1873 gene product reveals limited similarity to a repeated motif that is found in a variety of other proteins. While not a novel fold, it serves as a model for orthologues predicted to be related by sequence and it is hoped that knowledge of the structure of Rv1873 will aid in determining a possible function for this protein.
- Published
- 2006
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