A novel member of the YchN-like fold: solution structure of the hypothetical protein Tm0979 from Thermotoga maritima
| Autor: | Bin Wu, Elizabeth M. Meiering, Adelinda Yee, Gabriela Meglei, Cheryl H. Arrowsmith, Ricardo Stephen, Antonio Pineda-Lucena, Kenrick A. Vassall, Chengsong Liu, Peter B. Stathopulos, Joe A. Gaspar |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
Models
Molecular Proteomics Protein Folding Molecular Sequence Data Thioredoxin fold Crystallography X-Ray Biochemistry Protein Structure Secondary Protein structure Bacterial Proteins TIM barrel Thermotoga maritima Amino Acid Sequence Protein Structure Quaternary Molecular Biology Nuclear Magnetic Resonance Biomolecular biology Sequence Homology Amino Acid Flavodoxin fold Ferredoxin fold biology.organism_classification Globin fold Protein Structure Tertiary Solutions Crystallography Protein Subunits Protein Structure Report Protein folding Dimerization Sequence Alignment |
| Zdroj: | Protein science : a publication of the Protein Society. 14(1) |
| ISSN: | 0961-8368 |
| Popis: | We report herein the NMR structure of Tm0979, a structural proteomics target from Thermotoga maritima. The Tm0979 fold consists of four beta/alpha units, which form a central parallel beta-sheet with strand order 1234. The first three helices pack toward one face of the sheet and the fourth helix packs against the other face. The protein forms a dimer by adjacent parallel packing of the fourth helices sandwiched between the two beta-sheets. This fold is very interesting from several points of view. First, it represents the first structure determination for the DsrH family of conserved hypothetical proteins, which are involved in oxidation of intracellular sulfur but have no defined molecular function. Based on structure and sequence analysis, possible functions are discussed. Second, the fold of Tm0979 most closely resembles YchN-like folds; however the proteins that adopt these folds differ in secondary structural elements and quaternary structure. Comparison of these proteins provides insight into possible mechanisms of evolution of quaternary structure through a simple mechanism of hydrophobicity-changing mutations of one or two residues. Third, the Tm0979 fold is found to be similar to flavodoxin-like folds and beta/alpha barrel proteins, and may provide a link between these very abundant folds and putative ancestral half-barrel proteins. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text