1X9A

Solution NMR Structure of Protein Tm0979 from Thermotoga maritima. Ontario Center for Structural Proteomics Target TM0979_1_87; Northeast Structural Genomics Consortium Target VT98.

Summary for 1X9A

• Entry DOI: 10.2210/pdb1x9a/pdb
• NMR Information: BMRB: 6324
• Descriptor: hypothetical protein TM0979 (1 entity in total)
• Functional Keywords: structural genomics, protein structure initiative, psi, northeast structural genomics consortium, nesg, ocsp, hypothetical protein, beta-alpha protein, dimer, unknown function
• Biological source: Thermotoga maritima
• Total number of polymer chains: 2
• Total formula weight: 24119.41

Authors

Gaspar, J.A.,Liu, C.,Vassall, K.A.,Stathopulos, P.B.,Meglei, G.,Stephen, R.,Pineda-Lucena, A.,Wu, B.,Yee, A.,Arrowsmith, C.H.,Meiering, E.M.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2004-08-20, release date: 2004-12-07, Last modification date: 2024-05-22)

Primary citation

Gaspar, J.A.,Liu, C.,Vassall, K.A.,Meglei, G.,Stephen, R.,Stathopulos, P.B.,Pineda-Lucena, A.,Wu, B.,Yee, A.,Arrowsmith, C.H.,Meiering, E.M.
A novel member of the YchN-like fold: solution structure of the hypothetical protein Tm0979 from Thermotoga maritima.
Protein Sci., 14:216-223, 2005

PubMed Abstract: 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.

PubMed: 15608123
DOI: 10.1110/ps.041068605

Experimental method

SOLUTION NMR